α chymotrypsin  (Millipore)

 
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    Name:
    Chymotrypsin
    Description:
    This product is provided as delivered and specified by the issuing Pharmacopoeia All information provided in support of this product including SDS and any product information leaflets have been developed and issued under the Authority of the Issuing Pharmacopoeia For further information and support please go to the website of the issuing Pharmacopoeia
    Catalog Number:
    C2160000
    Price:
    None
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    Structured Review

    Millipore α chymotrypsin
    Gel exclusion chromatography of GfoR and GfoR∶GfoA complexes. Proteins were purified from strain MA8731 containing the GfoR plasmid pSEB11 as described in Materials and Methods . The strain was grown without (A) or with arabinose (B). About 10 µg of each protein preparation were applied to an Amersham Sephadex G75 column. 0.5 mL fractions were collected after the passage of the void volume, dried, resuspended in protein loading buffer and separated on a 12% SDS-polyacrylamide gel. Band identification was confirmed by anti-FLAG Western blotting (data not shown). The column was size-calibrated using <t>α-chymotrypsin,</t> ovalbumin and bovine serum albumin from Sigma-Aldrich.
    This product is provided as delivered and specified by the issuing Pharmacopoeia All information provided in support of this product including SDS and any product information leaflets have been developed and issued under the Authority of the Issuing Pharmacopoeia For further information and support please go to the website of the issuing Pharmacopoeia
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    Images

    1) Product Images from "Bacteriophage Crosstalk: Coordination of Prophage Induction by Trans-Acting Antirepressors"

    Article Title: Bacteriophage Crosstalk: Coordination of Prophage Induction by Trans-Acting Antirepressors

    Journal: PLoS Genetics

    doi: 10.1371/journal.pgen.1002149

    Gel exclusion chromatography of GfoR and GfoR∶GfoA complexes. Proteins were purified from strain MA8731 containing the GfoR plasmid pSEB11 as described in Materials and Methods . The strain was grown without (A) or with arabinose (B). About 10 µg of each protein preparation were applied to an Amersham Sephadex G75 column. 0.5 mL fractions were collected after the passage of the void volume, dried, resuspended in protein loading buffer and separated on a 12% SDS-polyacrylamide gel. Band identification was confirmed by anti-FLAG Western blotting (data not shown). The column was size-calibrated using α-chymotrypsin, ovalbumin and bovine serum albumin from Sigma-Aldrich.
    Figure Legend Snippet: Gel exclusion chromatography of GfoR and GfoR∶GfoA complexes. Proteins were purified from strain MA8731 containing the GfoR plasmid pSEB11 as described in Materials and Methods . The strain was grown without (A) or with arabinose (B). About 10 µg of each protein preparation were applied to an Amersham Sephadex G75 column. 0.5 mL fractions were collected after the passage of the void volume, dried, resuspended in protein loading buffer and separated on a 12% SDS-polyacrylamide gel. Band identification was confirmed by anti-FLAG Western blotting (data not shown). The column was size-calibrated using α-chymotrypsin, ovalbumin and bovine serum albumin from Sigma-Aldrich.

    Techniques Used: Chromatography, Purification, Plasmid Preparation, Western Blot

    2) Product Images from "Mitochondrial Thioredoxin System as a Modulator of Cyclophilin D Redox State"

    Article Title: Mitochondrial Thioredoxin System as a Modulator of Cyclophilin D Redox State

    Journal: Scientific Reports

    doi: 10.1038/srep23071

    PPIase activity of CypD in the mitochondrial matrix. Mitochondrial matrix (30 μg proteins) was preincubated in 100 mM NaCl, 50 mM HEPES/Tris (pH 8.0) at 25 °C for 15 min in the presence, where indicated, of 300 μM NADPH, 0.4 μM TrxR1, 3 μM Trx from E. coli or 1 μM auranofin (AF). PPIase activity was estimated by a coupled assay utilizing α-chymotrypsin as described under Methods. ( A ) time course of PPIase activity in different experimental conditions and ( B ) first-order rate constants (s -1 ) indicated in the ordinate axis (*p
    Figure Legend Snippet: PPIase activity of CypD in the mitochondrial matrix. Mitochondrial matrix (30 μg proteins) was preincubated in 100 mM NaCl, 50 mM HEPES/Tris (pH 8.0) at 25 °C for 15 min in the presence, where indicated, of 300 μM NADPH, 0.4 μM TrxR1, 3 μM Trx from E. coli or 1 μM auranofin (AF). PPIase activity was estimated by a coupled assay utilizing α-chymotrypsin as described under Methods. ( A ) time course of PPIase activity in different experimental conditions and ( B ) first-order rate constants (s -1 ) indicated in the ordinate axis (*p

    Techniques Used: Activity Assay

    3) Product Images from "Intracellular activation of ovastacin mediates pre-fertilization hardening of the zona pellucida"

    Article Title: Intracellular activation of ovastacin mediates pre-fertilization hardening of the zona pellucida

    Journal: Molecular Human Reproduction

    doi: 10.1093/molehr/gax040

    Effect of ovastacin on zona pellucida hardening, ZP2 cleavage and fertilization rate ( A ) α-chymotrypsin zona pellucida (ZP) digestion of wild-type oocytes (+/+), ovastacin-deficient (−/−) oocytes and 2-cell embryos. ◦ = outlier; n : total oocytes. Addition of fetuin-B (2.5 μM), pefabloc (250 μM) and E64 (50 μM) was simultaneous to the activation of oocytes by Ca 2+ ionophore (2.5 μM). All experiments are statistically significant ( P
    Figure Legend Snippet: Effect of ovastacin on zona pellucida hardening, ZP2 cleavage and fertilization rate ( A ) α-chymotrypsin zona pellucida (ZP) digestion of wild-type oocytes (+/+), ovastacin-deficient (−/−) oocytes and 2-cell embryos. ◦ = outlier; n : total oocytes. Addition of fetuin-B (2.5 μM), pefabloc (250 μM) and E64 (50 μM) was simultaneous to the activation of oocytes by Ca 2+ ionophore (2.5 μM). All experiments are statistically significant ( P

    Techniques Used: Activation Assay

    4) Product Images from "Facile Synthesis of Bis(indolyl)methanes Catalyzed by α-Chymotrypsin"

    Article Title: Facile Synthesis of Bis(indolyl)methanes Catalyzed by α-Chymotrypsin

    Journal: Molecules

    doi: 10.3390/molecules191219665

    α-Chymotrypsin-catalyzed tandem reaction of indole and aldehydes.
    Figure Legend Snippet: α-Chymotrypsin-catalyzed tandem reaction of indole and aldehydes.

    Techniques Used:

    Proposed mechanism for α-chymotrypsin-catalyzed cascade reaction.
    Figure Legend Snippet: Proposed mechanism for α-chymotrypsin-catalyzed cascade reaction.

    Techniques Used:

    5) Product Images from "EC-QCL mid-IR transmission spectroscopy for monitoring dynamic changes of protein secondary structure in aqueous solution on the example of β-aggregation in alcohol-denaturated α-chymotrypsin"

    Article Title: EC-QCL mid-IR transmission spectroscopy for monitoring dynamic changes of protein secondary structure in aqueous solution on the example of β-aggregation in alcohol-denaturated α-chymotrypsin

    Journal: Analytical and Bioanalytical Chemistry

    doi: 10.1007/s00216-016-9464-5

    a Time-dependent IR absorbance and b second-derivative spectra of 20 mg mL −1 α-chymotrypsin in 50 % TFE/buffer solution, pH 7.8 at 25 °C ( solid lines ). The spectra were recorded at time periods between 2 and 240 min (times as indicated in the graph) after the protein was dissolved in TFE/buffer. Blue solid lines show the spectrum of aCT with TFE-induced α-helical structure. Green solid lines indicate the spectrum of the protein after gradual formation of intermolecular β-sheets. Grey dashed lines represent spectra of the native protein in aqueous buffer. Black arrows illustrate directions of absorbance changes as a function of time
    Figure Legend Snippet: a Time-dependent IR absorbance and b second-derivative spectra of 20 mg mL −1 α-chymotrypsin in 50 % TFE/buffer solution, pH 7.8 at 25 °C ( solid lines ). The spectra were recorded at time periods between 2 and 240 min (times as indicated in the graph) after the protein was dissolved in TFE/buffer. Blue solid lines show the spectrum of aCT with TFE-induced α-helical structure. Green solid lines indicate the spectrum of the protein after gradual formation of intermolecular β-sheets. Grey dashed lines represent spectra of the native protein in aqueous buffer. Black arrows illustrate directions of absorbance changes as a function of time

    Techniques Used: Activated Clotting Time Assay

    6) Product Images from "Release of FGF1 and p40 synaptotagmin 1 correlates with their membrane destabilizing ability."

    Article Title: Release of FGF1 and p40 synaptotagmin 1 correlates with their membrane destabilizing ability.

    Journal: Biochemical and biophysical research communications

    doi: 10.1016/j.bbrc.2006.08.021

    The release of carboxyfluorescein (CF) from pL liposomes by FGF1, S100A13, and p40 Syt1 Liposomes were prepared using pS, pG, pI, or pC in the presence of CF. The release of CF after the addition of 1 mM (○-○), 500 nM (Δ-Δ), 250 nM (x-x), 125 nM (⋄-⋄) of recombinant FGF1, S100A13, and p40 Syt1 was continuously monitored using a fluorescence spectrophotometer (excitation:470 nm; emission:520 nm). The data are reported as a function of time in seconds. 1 mM α-chymotrypsin (—) or 0.1% Triton X100 (•-•) were used as respectively negative and positive controls of membrane destabiliization. The pL concentration in the cuvette was 2 μM.
    Figure Legend Snippet: The release of carboxyfluorescein (CF) from pL liposomes by FGF1, S100A13, and p40 Syt1 Liposomes were prepared using pS, pG, pI, or pC in the presence of CF. The release of CF after the addition of 1 mM (○-○), 500 nM (Δ-Δ), 250 nM (x-x), 125 nM (⋄-⋄) of recombinant FGF1, S100A13, and p40 Syt1 was continuously monitored using a fluorescence spectrophotometer (excitation:470 nm; emission:520 nm). The data are reported as a function of time in seconds. 1 mM α-chymotrypsin (—) or 0.1% Triton X100 (•-•) were used as respectively negative and positive controls of membrane destabiliization. The pL concentration in the cuvette was 2 μM.

    Techniques Used: Recombinant, Fluorescence, Spectrophotometry, Concentration Assay

    7) Product Images from "PROSTATE-SPECIFIC ANTIGEN IS A "CHYMOTRYPSIN-LIKE" SERINE PROTEASE WITH UNIQUE P1 SUBSTRATE SPECIFICITY"

    Article Title: PROSTATE-SPECIFIC ANTIGEN IS A "CHYMOTRYPSIN-LIKE" SERINE PROTEASE WITH UNIQUE P1 SUBSTRATE SPECIFICITY

    Journal: Biochemistry

    doi: 10.1021/bi9001858

    Surface representation of the S1 pocket of PSA ( left ) and bovine α-chymotrypsin ( right ). The P1 tyrosine residue is shown as a yellow ball-and-stick model. The polar hydroxyl moiety of the bound residue is depicted in purple. Surface colors represent
    Figure Legend Snippet: Surface representation of the S1 pocket of PSA ( left ) and bovine α-chymotrypsin ( right ). The P1 tyrosine residue is shown as a yellow ball-and-stick model. The polar hydroxyl moiety of the bound residue is depicted in purple. Surface colors represent

    Techniques Used:

    A, Sequence alignment of the 15 human kallikreins and bovine α-chymotrypsin. Only the residues spanning the S1 pocket of serine proteases are presented. The residues highlighted in yellow are critical for the P1 specificities of respective protease.
    Figure Legend Snippet: A, Sequence alignment of the 15 human kallikreins and bovine α-chymotrypsin. Only the residues spanning the S1 pocket of serine proteases are presented. The residues highlighted in yellow are critical for the P1 specificities of respective protease.

    Techniques Used: Sequencing

    8) Product Images from "Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients"

    Article Title: Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients

    Journal: Scientia Pharmaceutica

    doi: 10.3797/scipharm.1501-12

    Degradation of mAb 85 by proteases as analysed by SEC: (A) Retention time shift after incubation with α-chymotrypsin, papain, or pepsin; (B) Fragmentation after incubation with the proteases (i) papain and (ii) pepsin. The proteolytic activity of all tested proteases is significantly reduced by adding sorbitol or glycine
    Figure Legend Snippet: Degradation of mAb 85 by proteases as analysed by SEC: (A) Retention time shift after incubation with α-chymotrypsin, papain, or pepsin; (B) Fragmentation after incubation with the proteases (i) papain and (ii) pepsin. The proteolytic activity of all tested proteases is significantly reduced by adding sorbitol or glycine

    Techniques Used: Size-exclusion Chromatography, Incubation, Activity Assay

    9) Product Images from "Effect of potassium channel openers in acute and chronic models of glaucoma"

    Article Title: Effect of potassium channel openers in acute and chronic models of glaucoma

    Journal: Taiwan Journal of Ophthalmology

    doi: 10.1016/j.tjo.2016.05.006

    Effect of nicorandil (1%), [glibenclamide (1%) + nicorandil (1%)], [pilocarine (1%) + nicorandil (1%)], [indomethacine (1%) + nicorandil (1%)], and pilocarpine (1%) on IOP in rabbits with α-chymotrypsin-induced ocular hypertension. Each point and bar represents mean ± SEM of six observations. * Significantly different from control ( p
    Figure Legend Snippet: Effect of nicorandil (1%), [glibenclamide (1%) + nicorandil (1%)], [pilocarine (1%) + nicorandil (1%)], [indomethacine (1%) + nicorandil (1%)], and pilocarpine (1%) on IOP in rabbits with α-chymotrypsin-induced ocular hypertension. Each point and bar represents mean ± SEM of six observations. * Significantly different from control ( p

    Techniques Used:

    Effect of pinacidil (1%), [glibenclamide (1%) + pinacidil (1%)], [pilocarine (1%) + pinacidil (1%)], [indomethacine (1%) + pinacidil (1%)], and pilocarpine (1%) on IOP in rabbits with α-chymotrypsin-induced ocular hypertension. Each point and bar represents mean ± standard error of the mean of six observations. * Significantly different from control ( p
    Figure Legend Snippet: Effect of pinacidil (1%), [glibenclamide (1%) + pinacidil (1%)], [pilocarine (1%) + pinacidil (1%)], [indomethacine (1%) + pinacidil (1%)], and pilocarpine (1%) on IOP in rabbits with α-chymotrypsin-induced ocular hypertension. Each point and bar represents mean ± standard error of the mean of six observations. * Significantly different from control ( p

    Techniques Used:

    10) Product Images from "Development of an aptamer-based affinity purification method for vascular endothelial growth factor"

    Article Title: Development of an aptamer-based affinity purification method for vascular endothelial growth factor

    Journal: Biotechnology Reports

    doi: 10.1016/j.btre.2015.08.006

    Characterization of aptamer target binding via microscale thermophoresis and electrophoresis mobility shift assay (EMSA). Left: saturation curve of V7t1 aptamer and VEGF. Cy3-labeled V7t1 was incubated with different concentrations of VEGF and afterwards analyzed by microscale thermophoresis as three-fold replicates. A K D of 75.9 nM ± 13.0 nM was determined for this interaction. Right: analysis of aptamer binding to the target protein VEGF and the non-target proteins myoglobin (Myo), α-chymotrypsin (Chy) and bovine serum albumin (BSA) via EMSA. The Cy3-labeled aptamer V7t1 was incubated with an excess of protein, respectively. Afterwards the samples were analyzed by agarose gel electrophoresis. Pure VEGF and V7t1 were used as negative controls, respectively. Results of the EMSA demonstrate a specific binding of V7t1 to VEGF in comparison to the other tested proteins.
    Figure Legend Snippet: Characterization of aptamer target binding via microscale thermophoresis and electrophoresis mobility shift assay (EMSA). Left: saturation curve of V7t1 aptamer and VEGF. Cy3-labeled V7t1 was incubated with different concentrations of VEGF and afterwards analyzed by microscale thermophoresis as three-fold replicates. A K D of 75.9 nM ± 13.0 nM was determined for this interaction. Right: analysis of aptamer binding to the target protein VEGF and the non-target proteins myoglobin (Myo), α-chymotrypsin (Chy) and bovine serum albumin (BSA) via EMSA. The Cy3-labeled aptamer V7t1 was incubated with an excess of protein, respectively. Afterwards the samples were analyzed by agarose gel electrophoresis. Pure VEGF and V7t1 were used as negative controls, respectively. Results of the EMSA demonstrate a specific binding of V7t1 to VEGF in comparison to the other tested proteins.

    Techniques Used: Binding Assay, Microscale Thermophoresis, Electrophoresis, Mobility Shift, Labeling, Incubation, Agarose Gel Electrophoresis

    11) Product Images from "Dromedary Milk Protein Hydrolysates Show Enhanced Antioxidant and Functional Properties"

    Article Title: Dromedary Milk Protein Hydrolysates Show Enhanced Antioxidant and Functional Properties

    Journal: Food Technology and Biotechnology

    doi: 10.17113/ftb.58.02.20.6337

    Degree of hydrolysis (DH) of dromedary milk proteins (DMPH) treated with pepsin (DMPH-Pep), trypsin (DMPH-Try), α-chymotrypsin (DMPH-Chy), pancreatin (DMPH-Pan), papain (DMPH-Pap) and pronase (DMPH-Pro)
    Figure Legend Snippet: Degree of hydrolysis (DH) of dromedary milk proteins (DMPH) treated with pepsin (DMPH-Pep), trypsin (DMPH-Try), α-chymotrypsin (DMPH-Chy), pancreatin (DMPH-Pan), papain (DMPH-Pap) and pronase (DMPH-Pro)

    Techniques Used:

    Reversed phase-HPLC profiles of undigested dromedary milk proteins (UDMP) and their hydrolysates (DMPHs): a) UDMP, with b) pepsin, c) trypsin, d) α-chymotrypsin, e) pancreatin, f) papain and g) pronase
    Figure Legend Snippet: Reversed phase-HPLC profiles of undigested dromedary milk proteins (UDMP) and their hydrolysates (DMPHs): a) UDMP, with b) pepsin, c) trypsin, d) α-chymotrypsin, e) pancreatin, f) papain and g) pronase

    Techniques Used: High Performance Liquid Chromatography

    12) Product Images from "Separation and identification of bioactive peptides from stem of Tinospora cordifolia (Willd.) Miers"

    Article Title: Separation and identification of bioactive peptides from stem of Tinospora cordifolia (Willd.) Miers

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0193717

    Analyzes on enzyme digests. (A) Tricine SDS-PAGE (14%) of T . cordifolia stem proteins treated with papain enzyme. Lane 1, marker (GeNei low molecular weight); lane 2, protein not treated with enzyme; lanes 3 to 7, protein treated with papain enzyme for different time intervals of 30 to 120 minutes; (B) Tricine SDS-PAGE (14%) of T . cordifolia stem proteins treated with trypsin enzyme. Lane 1, marker (GeNei low molecular weight); lane 2, protein not treated with an enzyme; lanes 3 to 7, protein treated with trypsin enzyme for time intervals of 30 to 120 minutes; (C) Tricine SDS-PAGE (14%) of T . cordifolia stem proteins treated with the α-chymotrypsin enzyme. Lane 1, marker (GeNei low molecular weight); lane 2, protein not treated with an enzyme; lanes 3 to 7, protein treated with the α-chymotrypsin enzyme for different time intervals of 30 to 120 minutes; (D) Tricine SDS-PAGE (14%) of T . cordifolia stem proteins treated with pepsin enzyme with silver staining. Lane 1, marker (GeNei low molecular weight); lane 2, protein not treated with the enzyme; lane 3, enzyme alone; lanes 4 to 7, protein treated with pepsin enzyme for different time intervals of 60 and 120 minutes, with two different enzyme:protein ratios of 1:3.33 and 1:6.67 (wt/wt); (E) Tricine SDS-PAGE (14%) of T . cordifolia stem proteins treated with pepsin-pancreatin enzymes with silver staining. Lane 1, marker (GeNei low molecular weight); lane 2, protein not treated with an enzyme; lane 3, enzyme alone; lane 4, protein treated with pepsin-pancreatin enzyme for 2 and 4 hours.
    Figure Legend Snippet: Analyzes on enzyme digests. (A) Tricine SDS-PAGE (14%) of T . cordifolia stem proteins treated with papain enzyme. Lane 1, marker (GeNei low molecular weight); lane 2, protein not treated with enzyme; lanes 3 to 7, protein treated with papain enzyme for different time intervals of 30 to 120 minutes; (B) Tricine SDS-PAGE (14%) of T . cordifolia stem proteins treated with trypsin enzyme. Lane 1, marker (GeNei low molecular weight); lane 2, protein not treated with an enzyme; lanes 3 to 7, protein treated with trypsin enzyme for time intervals of 30 to 120 minutes; (C) Tricine SDS-PAGE (14%) of T . cordifolia stem proteins treated with the α-chymotrypsin enzyme. Lane 1, marker (GeNei low molecular weight); lane 2, protein not treated with an enzyme; lanes 3 to 7, protein treated with the α-chymotrypsin enzyme for different time intervals of 30 to 120 minutes; (D) Tricine SDS-PAGE (14%) of T . cordifolia stem proteins treated with pepsin enzyme with silver staining. Lane 1, marker (GeNei low molecular weight); lane 2, protein not treated with the enzyme; lane 3, enzyme alone; lanes 4 to 7, protein treated with pepsin enzyme for different time intervals of 60 and 120 minutes, with two different enzyme:protein ratios of 1:3.33 and 1:6.67 (wt/wt); (E) Tricine SDS-PAGE (14%) of T . cordifolia stem proteins treated with pepsin-pancreatin enzymes with silver staining. Lane 1, marker (GeNei low molecular weight); lane 2, protein not treated with an enzyme; lane 3, enzyme alone; lane 4, protein treated with pepsin-pancreatin enzyme for 2 and 4 hours.

    Techniques Used: SDS Page, Marker, Molecular Weight, Silver Staining

    Comparison of percentage reduction of DPPH. (A) by different concentrations of T . cordifolia stem proteins and same concentrations of Ascorbic acid; (B) by T . cordifolia stem proteins hydrolyzed in vitro for various time intervals by different gastrointestinal enzymes (Papain, Trypsin, α-Chymotrypsin, and Pepsin).
    Figure Legend Snippet: Comparison of percentage reduction of DPPH. (A) by different concentrations of T . cordifolia stem proteins and same concentrations of Ascorbic acid; (B) by T . cordifolia stem proteins hydrolyzed in vitro for various time intervals by different gastrointestinal enzymes (Papain, Trypsin, α-Chymotrypsin, and Pepsin).

    Techniques Used: In Vitro

    Relative activity of trypsin and α-chymotrypsin after a pre-incubation of 90 minutes with varying amounts of T . cordifolia proteins. (A) Increase in Trypsin enzyme inhibition with increase in amount of protein; (B) Increase in α-Chymotrypsin enzyme inhibition with increase in amount of protein.
    Figure Legend Snippet: Relative activity of trypsin and α-chymotrypsin after a pre-incubation of 90 minutes with varying amounts of T . cordifolia proteins. (A) Increase in Trypsin enzyme inhibition with increase in amount of protein; (B) Increase in α-Chymotrypsin enzyme inhibition with increase in amount of protein.

    Techniques Used: Activity Assay, Incubation, Enzyme Inhibition Assay

    Disc diffusion plate assay showing T . cordifolia stem proteins’ effect on trypsin and α-chymotrypsin activity. The wells contained 5 ug of enzyme with varying amounts of proteins. A: Stem proteins incubated with trypsin; B: Both stem proteins and STI incubated with trypsin. C: Stem proteins incubated with α-chymotrypsin. +ive, 5 μg enzyme; -ive, 50 mM Tris-HCl buffer (pH 8.0); P, Protein sample (5 μg); 5, 5 μg enzyme + 5 μg protein (E:S = 1:1); 2.5, 5 μg enzyme + 2.5 μg protein (E:S = 2:1); 1.5, 5 μg enzyme + 1.5 μg protein (E:S = 3.33:1); 1, 5 μg enzyme + 1 μg protein (E:S = 5:1); 0.75, 5 μg enzyme + 0.75 μg protein (E:S = 6.67:1); 0.5, 5 μg enzyme + 0.5 μg protein (E:S = 10:1); STI, 5 μg enzyme + 1.5 μg Soybean Trypsin Inhibitor.
    Figure Legend Snippet: Disc diffusion plate assay showing T . cordifolia stem proteins’ effect on trypsin and α-chymotrypsin activity. The wells contained 5 ug of enzyme with varying amounts of proteins. A: Stem proteins incubated with trypsin; B: Both stem proteins and STI incubated with trypsin. C: Stem proteins incubated with α-chymotrypsin. +ive, 5 μg enzyme; -ive, 50 mM Tris-HCl buffer (pH 8.0); P, Protein sample (5 μg); 5, 5 μg enzyme + 5 μg protein (E:S = 1:1); 2.5, 5 μg enzyme + 2.5 μg protein (E:S = 2:1); 1.5, 5 μg enzyme + 1.5 μg protein (E:S = 3.33:1); 1, 5 μg enzyme + 1 μg protein (E:S = 5:1); 0.75, 5 μg enzyme + 0.75 μg protein (E:S = 6.67:1); 0.5, 5 μg enzyme + 0.5 μg protein (E:S = 10:1); STI, 5 μg enzyme + 1.5 μg Soybean Trypsin Inhibitor.

    Techniques Used: Diffusion-based Assay, Activity Assay, Incubation

    13) Product Images from "Comparison of Allergic Parameters between Whey Protein Concentrate and Its Hydrolysate in Rat Basophilic Leukemia (RBL)-2H3 Cells"

    Article Title: Comparison of Allergic Parameters between Whey Protein Concentrate and Its Hydrolysate in Rat Basophilic Leukemia (RBL)-2H3 Cells

    Journal: Korean Journal for Food Science of Animal Resources

    doi: 10.5851/kosfa.2018.e16

    Time course of whey protein concentrate (WPC) hydrolysis by trypsin and α-chymotrypsin. Values are mean of three replicate means (n=3)±SD. The different letters indicate statistically significant differences (p
    Figure Legend Snippet: Time course of whey protein concentrate (WPC) hydrolysis by trypsin and α-chymotrypsin. Values are mean of three replicate means (n=3)±SD. The different letters indicate statistically significant differences (p

    Techniques Used:

    SDS-PAGE patterns of whey protein concentrate (WPC) hydrolysates produced by trypsin and α-chymotrypsin after 8 h-hydrolysis. Lane 1, protein marker; Lane 2, WPC (40 µg/20 µL); Lane 3, WPC (80 µg/20 µL); Lane 4, WPC (120 µg/20 µL); Lane 5, WPC hydrolysate (40 µg/20 µL); Lane 6, WPC hydrolysate (80 µg/20 µL); Lane 7, WPC hydrolysate (120 µg/20 µL). SDS-PAGE, sodium dodecyl sulfate polyacrylamide gel electrophoresis.
    Figure Legend Snippet: SDS-PAGE patterns of whey protein concentrate (WPC) hydrolysates produced by trypsin and α-chymotrypsin after 8 h-hydrolysis. Lane 1, protein marker; Lane 2, WPC (40 µg/20 µL); Lane 3, WPC (80 µg/20 µL); Lane 4, WPC (120 µg/20 µL); Lane 5, WPC hydrolysate (40 µg/20 µL); Lane 6, WPC hydrolysate (80 µg/20 µL); Lane 7, WPC hydrolysate (120 µg/20 µL). SDS-PAGE, sodium dodecyl sulfate polyacrylamide gel electrophoresis.

    Techniques Used: SDS Page, Produced, Marker, Polyacrylamide Gel Electrophoresis

    14) Product Images from "Pharmacokinetic study of niosome-loaded insulin in diabetic rats"

    Article Title: Pharmacokinetic study of niosome-loaded insulin in diabetic rats

    Journal: DARU Journal of Pharmaceutical Sciences

    doi:

    The insulin protection property (mean of±SD) of different niosomes against proteolytic effects of digestive enzymes in vitro . Vesicular preparations were incubated with α-chymotrypsin and trypsin solutions for 3 hrs and with pepsin solution for one hour at 37°C ( n =3).
    Figure Legend Snippet: The insulin protection property (mean of±SD) of different niosomes against proteolytic effects of digestive enzymes in vitro . Vesicular preparations were incubated with α-chymotrypsin and trypsin solutions for 3 hrs and with pepsin solution for one hour at 37°C ( n =3).

    Techniques Used: In Vitro, Incubation

    15) Product Images from "Stability Studies of the Vaccine Adjuvant U-Omp19"

    Article Title: Stability Studies of the Vaccine Adjuvant U-Omp19

    Journal: Journal of Pharmaceutical Sciences

    doi: 10.1016/j.xphs.2020.10.011

    Impact of multiple freeze-thaw cycles on U-Omp19 stability. Samples of U-Omp19 were subjected to multiple freeze and thaw cycles. (a) SDS–PAGE Coomassie stained gels of non-reduced U-Omp19 samples after 0 (lane 2) to 6 (lane 8) freeze-thaw cycles. Lane 1: Molecular Weight Markers (MWM). (b) Percentage of α-chymotrypsin proteolytic activity remaining upon incubation with buffer (No inhibitor) or 50 μM of each U-Omp19 sample after 0 to 6 freeze-thaw cycles. (c) Dynamic light scattering measurements: Representative particle size distribution profiles by intensity and volume for U-Omp19 samples without freezing (Cycle 0) or after 1 or 6 freeze-thaw cycles.
    Figure Legend Snippet: Impact of multiple freeze-thaw cycles on U-Omp19 stability. Samples of U-Omp19 were subjected to multiple freeze and thaw cycles. (a) SDS–PAGE Coomassie stained gels of non-reduced U-Omp19 samples after 0 (lane 2) to 6 (lane 8) freeze-thaw cycles. Lane 1: Molecular Weight Markers (MWM). (b) Percentage of α-chymotrypsin proteolytic activity remaining upon incubation with buffer (No inhibitor) or 50 μM of each U-Omp19 sample after 0 to 6 freeze-thaw cycles. (c) Dynamic light scattering measurements: Representative particle size distribution profiles by intensity and volume for U-Omp19 samples without freezing (Cycle 0) or after 1 or 6 freeze-thaw cycles.

    Techniques Used: SDS Page, Staining, Molecular Weight, Activity Assay, Incubation

    Impact of lyophilization and long-term storage in solid state on protease inhibitor activity, protein integrity, and aggregation of U-Omp19. Samples of U-Omp19 were freeze dryed and placed for long term stability studies for up to 18 months at −80 °C, 4 °C, and 20 °C (RT). (a) Dynamic light scattering measurements: Comparison of particle size distribution profiles by intensity and volume for U-Omp19 samples without freeze drying (Control) or after lyophilization and instant reconstitution (t = 0). (b) SDS–PAGE Coomassie stained gel of reduced U-Omp19 samples. Lane 1: Molecular Weight Markers (MWM), Lane 2: U-Omp19 in aqueous solution (not lyophilized). Lane 3 to 5: lyophilized U-Omp19 after reconstitution stored in solid state for 18 months at the indicated temperatures. (c) Recovered inhibitor activity expressed as percentage of α-chymotrypsin proteolytic activity (mean ± SEM) remaining upon incubation with buffer (No inhibitor), 50 μM of U-Omp19 control sample (not lyophilized) or lyophilized and rehydrated U-Omp19 samples after storage in solid state for 18 months at indicated temperatures. ★★★: P
    Figure Legend Snippet: Impact of lyophilization and long-term storage in solid state on protease inhibitor activity, protein integrity, and aggregation of U-Omp19. Samples of U-Omp19 were freeze dryed and placed for long term stability studies for up to 18 months at −80 °C, 4 °C, and 20 °C (RT). (a) Dynamic light scattering measurements: Comparison of particle size distribution profiles by intensity and volume for U-Omp19 samples without freeze drying (Control) or after lyophilization and instant reconstitution (t = 0). (b) SDS–PAGE Coomassie stained gel of reduced U-Omp19 samples. Lane 1: Molecular Weight Markers (MWM), Lane 2: U-Omp19 in aqueous solution (not lyophilized). Lane 3 to 5: lyophilized U-Omp19 after reconstitution stored in solid state for 18 months at the indicated temperatures. (c) Recovered inhibitor activity expressed as percentage of α-chymotrypsin proteolytic activity (mean ± SEM) remaining upon incubation with buffer (No inhibitor), 50 μM of U-Omp19 control sample (not lyophilized) or lyophilized and rehydrated U-Omp19 samples after storage in solid state for 18 months at indicated temperatures. ★★★: P

    Techniques Used: Protease Inhibitor, Activity Assay, SDS Page, Staining, Molecular Weight, Incubation

    Impact of long-term storage on U-Omp19 protease inhibitor activity. Protease inhibitor activity was determined by an α-Chymotrypsin activity assay using a specific fluorogenic substrate in which the increment in fluorescence is proportional to proteolytic activity. α-Chymotrypsin was pre-incubated for 1 h with buffer (No inhibitor) or 50 μM of each U-Omp19 sample: fresh prepared (t = 0), or stored for different time periods (1 day or 1, 2, 3, 6, 9, 12, 18, 24 and 36 months) at the indicated temperatures (−80 °C, −20 °C, 4 °C, and 20 °C). Inhibitor activity is expressed as percentage of protease activity remaining when compared to “No inhibitor” condition (100% of activity). (a) Representative bar graph for the protease inhibitor activity analysis at time point = 36 months. Each bar represents the mean residual proteolytic activity of α-chymotrypsin and error bars represents SEM. ★★★: P
    Figure Legend Snippet: Impact of long-term storage on U-Omp19 protease inhibitor activity. Protease inhibitor activity was determined by an α-Chymotrypsin activity assay using a specific fluorogenic substrate in which the increment in fluorescence is proportional to proteolytic activity. α-Chymotrypsin was pre-incubated for 1 h with buffer (No inhibitor) or 50 μM of each U-Omp19 sample: fresh prepared (t = 0), or stored for different time periods (1 day or 1, 2, 3, 6, 9, 12, 18, 24 and 36 months) at the indicated temperatures (−80 °C, −20 °C, 4 °C, and 20 °C). Inhibitor activity is expressed as percentage of protease activity remaining when compared to “No inhibitor” condition (100% of activity). (a) Representative bar graph for the protease inhibitor activity analysis at time point = 36 months. Each bar represents the mean residual proteolytic activity of α-chymotrypsin and error bars represents SEM. ★★★: P

    Techniques Used: Protease Inhibitor, Activity Assay, Fluorescence, Incubation

    16) Product Images from "Barttin Regulates the Subcellular Localization and Posttranslational Modification of Human Cl-/H+ Antiporter ClC-5"

    Article Title: Barttin Regulates the Subcellular Localization and Posttranslational Modification of Human Cl-/H+ Antiporter ClC-5

    Journal: Frontiers in Physiology

    doi: 10.3389/fphys.2018.01490

    Interaction between ClC-5 and barttin in non-polarizing HEK293T cells. (A) Major expression sites of ClC-5 and ClC-K/barttin reported in the literature (PT, proximal tubule; tDL, thin descending limb of Henle’s loop; tAL and TAL, thin and thick ascending limbs of the Henle’s loop; DCT, distal convoluted tubule; CNT, connecting tubule; CCT, cortical collecting tubule; CD, collecting duct). (B) Alignment showing the sequence conservation of the protein region containing ClC-5 G261E, a Dent disease 1 mutation with Bartter-like phenotype (bold). (C) False-color representation of a fluorescent SDS-PAGE gel of HEK293T cell lysates containing expressed ClC-5-mYFP WT or ClC-5-mYFP G261E. Lysates were incubated with PNGaseF or EndoH to cleave all types or specifically the high mannose N-linked glycosylation, respectively. The resistance of ClC-5 to EndoH indicates complex glycosylation. (D) Representative confocal images of HEK293T cells expressing ClC-5 mCherry or barttin mCFP. Scale bars here and hereafter correspond to 10 μm. (E) Representative confocal image of HEK293T cells expressing ClC-5 G261E mCherry. (F,G) Representative confocal images of HEK293T cells coexpressing barttin (green) together with ClC-5 WT or ClC-5 G261E (ClC-5 in red). Magnified regions of interest are included as insets [in panel (F) , “i” denotes ER staining, whereas “ii” denotes staining of the perinuclear space]. (H) Grayscale presentation of a fluorescent SDS-PAGE gel of HEK293T cell lysates with expressed ClC-5-mCerulean or ClC-5-mCerulean G261E with or without coexpressed barttin mCherry. A brief exposure of intact cells to α-chymotrypsin was used to selectively cleave surface-exposed proteins. (I) Percentage of the low molecular ClC-5 protein band obtained from densitometry analysis of data as depicted in panel (H) , n = 7–11. The intensity of the lower band increases due to cleavage of surface exposed proteins by α-chymotrypsin and is proportional to the PM abundance of the investigated protein. (J) Percentage of the low molecular barttin protein band obtained from densitometry analysis of data as depicted in panel (H) , n = 7–11.
    Figure Legend Snippet: Interaction between ClC-5 and barttin in non-polarizing HEK293T cells. (A) Major expression sites of ClC-5 and ClC-K/barttin reported in the literature (PT, proximal tubule; tDL, thin descending limb of Henle’s loop; tAL and TAL, thin and thick ascending limbs of the Henle’s loop; DCT, distal convoluted tubule; CNT, connecting tubule; CCT, cortical collecting tubule; CD, collecting duct). (B) Alignment showing the sequence conservation of the protein region containing ClC-5 G261E, a Dent disease 1 mutation with Bartter-like phenotype (bold). (C) False-color representation of a fluorescent SDS-PAGE gel of HEK293T cell lysates containing expressed ClC-5-mYFP WT or ClC-5-mYFP G261E. Lysates were incubated with PNGaseF or EndoH to cleave all types or specifically the high mannose N-linked glycosylation, respectively. The resistance of ClC-5 to EndoH indicates complex glycosylation. (D) Representative confocal images of HEK293T cells expressing ClC-5 mCherry or barttin mCFP. Scale bars here and hereafter correspond to 10 μm. (E) Representative confocal image of HEK293T cells expressing ClC-5 G261E mCherry. (F,G) Representative confocal images of HEK293T cells coexpressing barttin (green) together with ClC-5 WT or ClC-5 G261E (ClC-5 in red). Magnified regions of interest are included as insets [in panel (F) , “i” denotes ER staining, whereas “ii” denotes staining of the perinuclear space]. (H) Grayscale presentation of a fluorescent SDS-PAGE gel of HEK293T cell lysates with expressed ClC-5-mCerulean or ClC-5-mCerulean G261E with or without coexpressed barttin mCherry. A brief exposure of intact cells to α-chymotrypsin was used to selectively cleave surface-exposed proteins. (I) Percentage of the low molecular ClC-5 protein band obtained from densitometry analysis of data as depicted in panel (H) , n = 7–11. The intensity of the lower band increases due to cleavage of surface exposed proteins by α-chymotrypsin and is proportional to the PM abundance of the investigated protein. (J) Percentage of the low molecular barttin protein band obtained from densitometry analysis of data as depicted in panel (H) , n = 7–11.

    Techniques Used: Expressing, Sequencing, Mutagenesis, SDS Page, Incubation, Staining

    17) Product Images from "Neuroregulation by vasoactive intestinal peptide (VIP) of mucus secretion in ferret trachea: activation of BKCa channels and inhibition of neurotransmitter release"

    Article Title: Neuroregulation by vasoactive intestinal peptide (VIP) of mucus secretion in ferret trachea: activation of BKCa channels and inhibition of neurotransmitter release

    Journal: British Journal of Pharmacology

    doi: 10.1038/sj.bjp.0702288

    Effect of endogenous vasoactive intestinal peptide (VIP) on acetylcholine (ACh) release in ferret tracheal strips in vitro . A VIP antibody (VIP-Ab, 1 : 500 dilution; a) or α-chymotrypsin (2 u ml −1 ; b) were used to exclude VIP. Tissues were pre-incubated with [ 3 H]-choline chloride (a marker for ACh) and stimulated electrically at 2.5 Hz, 50 V, 5 msec for 5 min. Data are mean per cent change in rate of [ 3 H] overflow at a second stimulation compared with the first stimulation for five animals per group; vertical bars are one s.e.mean. * P
    Figure Legend Snippet: Effect of endogenous vasoactive intestinal peptide (VIP) on acetylcholine (ACh) release in ferret tracheal strips in vitro . A VIP antibody (VIP-Ab, 1 : 500 dilution; a) or α-chymotrypsin (2 u ml −1 ; b) were used to exclude VIP. Tissues were pre-incubated with [ 3 H]-choline chloride (a marker for ACh) and stimulated electrically at 2.5 Hz, 50 V, 5 msec for 5 min. Data are mean per cent change in rate of [ 3 H] overflow at a second stimulation compared with the first stimulation for five animals per group; vertical bars are one s.e.mean. * P

    Techniques Used: In Vitro, Incubation, Marker

    18) Product Images from "Recognition of Malondialdehyde-modified Proteins by the C Terminus of Complement Factor H Is Mediated via the Polyanion Binding Site and Impaired by Mutations Found in Atypical Hemolytic Uremic Syndrome *"

    Article Title: Recognition of Malondialdehyde-modified Proteins by the C Terminus of Complement Factor H Is Mediated via the Polyanion Binding Site and Impaired by Mutations Found in Atypical Hemolytic Uremic Syndrome *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.527416

    Effect of proteolysis on the ability of MDA-ubiquitin to inhibit FH19–20 binding to MDA-BSA. A , MDA-ubiquitin was first incubated with α-chymotrypsin, and then the proteolysis was stopped with PMSF. Unproteolyzed MDA-ubiquitin with PMSF-inhibited
    Figure Legend Snippet: Effect of proteolysis on the ability of MDA-ubiquitin to inhibit FH19–20 binding to MDA-BSA. A , MDA-ubiquitin was first incubated with α-chymotrypsin, and then the proteolysis was stopped with PMSF. Unproteolyzed MDA-ubiquitin with PMSF-inhibited

    Techniques Used: Multiple Displacement Amplification, Binding Assay, Incubation

    19) Product Images from "High pressures increase α-chymotrypsin enzyme activity under perchlorate stress"

    Article Title: High pressures increase α-chymotrypsin enzyme activity under perchlorate stress

    Journal: Communications Biology

    doi: 10.1038/s42003-020-01279-4

    p, T -stability phase diagram of α-chymotrypsin. p , T -stability phase diagram of α-chymotrypsin (50 mg mL −1 , 10 mM CaCl 2 ). The lines indicate the transition curve, where Δ G u = 0, i.e., show the transition from the native to the (partially) unfolded state. The kinetic high-pressure stopped-flow (HPSF) measurements were performed in a region where the protein is well within the natively folded state. Error bars represent standard deviation.
    Figure Legend Snippet: p, T -stability phase diagram of α-chymotrypsin. p , T -stability phase diagram of α-chymotrypsin (50 mg mL −1 , 10 mM CaCl 2 ). The lines indicate the transition curve, where Δ G u = 0, i.e., show the transition from the native to the (partially) unfolded state. The kinetic high-pressure stopped-flow (HPSF) measurements were performed in a region where the protein is well within the natively folded state. Error bars represent standard deviation.

    Techniques Used: Standard Deviation

    Measuring α-chymotrypsin activity
    Figure Legend Snippet: Measuring α-chymotrypsin activity

    Techniques Used: Activity Assay

    α-Chymotrypsin activity curves. Michaelis–Menten plots of the enzymatic activity of α-CT at T = 20 °C in different buffer solutions at two selected pressures, 1 bar and 2 kbar. Error bars represent standard deviation.
    Figure Legend Snippet: α-Chymotrypsin activity curves. Michaelis–Menten plots of the enzymatic activity of α-CT at T = 20 °C in different buffer solutions at two selected pressures, 1 bar and 2 kbar. Error bars represent standard deviation.

    Techniques Used: Activity Assay, Standard Deviation

    Kinetic and volumetric parameters of α-chymotrypsin activity. a , c , e Pressure dependence of the kinetic parameters ( K M , k cat and k eff = k cat / K M ) of the α-CT-catalysed hydrolysis reaction of SP p NA in different salt conditions. b , d , f Each salt condition was normalised to its own kinetic parameter at 1 bar (starting point: 100%). Activation volume at high substrate concentrations, reflecting ( g ) the volume change responsible for k cat . Error bars represent standard deviation.
    Figure Legend Snippet: Kinetic and volumetric parameters of α-chymotrypsin activity. a , c , e Pressure dependence of the kinetic parameters ( K M , k cat and k eff = k cat / K M ) of the α-CT-catalysed hydrolysis reaction of SP p NA in different salt conditions. b , d , f Each salt condition was normalised to its own kinetic parameter at 1 bar (starting point: 100%). Activation volume at high substrate concentrations, reflecting ( g ) the volume change responsible for k cat . Error bars represent standard deviation.

    Techniques Used: Activity Assay, Activation Assay, Standard Deviation

    Changes to α-chymotrypsin FTIR spectra with pressure. Normalised pressure-dependent FTIR spectra of α-CT (50 mg mL −1 ) in ( a ) neat buffer (+10 mM CaCl 2 ) ( a ), ( c ) 0.25 M Mg(ClO 4 ) 2 and ( e ) at 35 °C, 0.5 M Mg(ClO 4 ) 2 at 25 °C, and the corresponding secondary structural changes ( b , d , f ) obtained from the curve fitting procedure. Arrows indicate increasing pressure and lines show the Boltzmann fits to the experimental data using Eq. ( 4 ).
    Figure Legend Snippet: Changes to α-chymotrypsin FTIR spectra with pressure. Normalised pressure-dependent FTIR spectra of α-CT (50 mg mL −1 ) in ( a ) neat buffer (+10 mM CaCl 2 ) ( a ), ( c ) 0.25 M Mg(ClO 4 ) 2 and ( e ) at 35 °C, 0.5 M Mg(ClO 4 ) 2 at 25 °C, and the corresponding secondary structural changes ( b , d , f ) obtained from the curve fitting procedure. Arrows indicate increasing pressure and lines show the Boltzmann fits to the experimental data using Eq. ( 4 ).

    Techniques Used:

    Changes to α-chymotrypsin FTIR spectra with temperature. Normalised temperature-dependent FTIR spectra of α-CT (50 mg mL −1 ) in neat buffer (+10 mM CaCl 2 ) ( a ), 0.25 M ( c ) and 0.5 M Mg(ClO 4 ) 2 ( e ) at ambient pressure and the corresponding secondary structural changes ( b , d , f ) obtained from the curve fitting procedure. Arrows indicate increasing temperature and the lines represent the Boltzmann fits to the experimental data using Eq. ( 3 ).
    Figure Legend Snippet: Changes to α-chymotrypsin FTIR spectra with temperature. Normalised temperature-dependent FTIR spectra of α-CT (50 mg mL −1 ) in neat buffer (+10 mM CaCl 2 ) ( a ), 0.25 M ( c ) and 0.5 M Mg(ClO 4 ) 2 ( e ) at ambient pressure and the corresponding secondary structural changes ( b , d , f ) obtained from the curve fitting procedure. Arrows indicate increasing temperature and the lines represent the Boltzmann fits to the experimental data using Eq. ( 3 ).

    Techniques Used:

    20) Product Images from "Comparison of Allergic Parameters between Whey Protein Concentrate and Its Hydrolysate in Rat Basophilic Leukemia (RBL)-2H3 Cells"

    Article Title: Comparison of Allergic Parameters between Whey Protein Concentrate and Its Hydrolysate in Rat Basophilic Leukemia (RBL)-2H3 Cells

    Journal: Korean Journal for Food Science of Animal Resources

    doi: 10.5851/kosfa.2018.e16

    Time course of whey protein concentrate (WPC) hydrolysis by trypsin and α-chymotrypsin. Values are mean of three replicate means (n=3)±SD. The different letters indicate statistically significant differences (p
    Figure Legend Snippet: Time course of whey protein concentrate (WPC) hydrolysis by trypsin and α-chymotrypsin. Values are mean of three replicate means (n=3)±SD. The different letters indicate statistically significant differences (p

    Techniques Used:

    SDS-PAGE patterns of whey protein concentrate (WPC) hydrolysates produced by trypsin and α-chymotrypsin after 8 h-hydrolysis. Lane 1, protein marker; Lane 2, WPC (40 µg/20 µL); Lane 3, WPC (80 µg/20 µL); Lane 4, WPC (120 µg/20 µL); Lane 5, WPC hydrolysate (40 µg/20 µL); Lane 6, WPC hydrolysate (80 µg/20 µL); Lane 7, WPC hydrolysate (120 µg/20 µL). SDS-PAGE, sodium dodecyl sulfate polyacrylamide gel electrophoresis.
    Figure Legend Snippet: SDS-PAGE patterns of whey protein concentrate (WPC) hydrolysates produced by trypsin and α-chymotrypsin after 8 h-hydrolysis. Lane 1, protein marker; Lane 2, WPC (40 µg/20 µL); Lane 3, WPC (80 µg/20 µL); Lane 4, WPC (120 µg/20 µL); Lane 5, WPC hydrolysate (40 µg/20 µL); Lane 6, WPC hydrolysate (80 µg/20 µL); Lane 7, WPC hydrolysate (120 µg/20 µL). SDS-PAGE, sodium dodecyl sulfate polyacrylamide gel electrophoresis.

    Techniques Used: SDS Page, Produced, Marker, Polyacrylamide Gel Electrophoresis

    21) Product Images from "Butylidenephthalide Blocks Potassium Channels and Enhances Basal Tension in Isolated Guinea-Pig Trachea"

    Article Title: Butylidenephthalide Blocks Potassium Channels and Enhances Basal Tension in Isolated Guinea-Pig Trachea

    Journal: BioMed Research International

    doi: 10.1155/2014/875230

    Inhibitory effects of atropine, FPL 55712, or pyrilamine 1  μ M (a), as well as pyrilamine 10  μ M or methysergide (b) and  α -chymotrypsin (c) on cumulative butylidenephthalide- (Bdph-) induced contraction of baseline tension in isolated guinea-pig trachea. All values are shown as mean ± SEM, and  n  is the number of experiments. There is no significant difference between test and respective control.
    Figure Legend Snippet: Inhibitory effects of atropine, FPL 55712, or pyrilamine 1  μ M (a), as well as pyrilamine 10  μ M or methysergide (b) and α -chymotrypsin (c) on cumulative butylidenephthalide- (Bdph-) induced contraction of baseline tension in isolated guinea-pig trachea. All values are shown as mean ± SEM, and n is the number of experiments. There is no significant difference between test and respective control.

    Techniques Used: Isolation

    22) Product Images from "Thermoresponsive Poly(N,N-diethylacrylamide-co-glycidyl methacrylate) Copolymers and Its Catalytically Active α-Chymotrypsin Bioconjugate with Enhanced Enzyme Stability"

    Article Title: Thermoresponsive Poly(N,N-diethylacrylamide-co-glycidyl methacrylate) Copolymers and Its Catalytically Active α-Chymotrypsin Bioconjugate with Enhanced Enzyme Stability

    Journal: Polymers

    doi: 10.3390/polym13060987

    Enzymatic activity ( A ) and the relative activity ( B ) of α-chymotrypsin (black) and the enzyme–polymer nanoparticle (red) as a function of pH.
    Figure Legend Snippet: Enzymatic activity ( A ) and the relative activity ( B ) of α-chymotrypsin (black) and the enzyme–polymer nanoparticle (red) as a function of pH.

    Techniques Used: Activity Assay

    DLS size distribution curves of the α-chymotrypsin (black), the P(DEAAm- co -GMA) copolymer (Sample C) (red) and the produced enzyme–polymer conjugate (blue).
    Figure Legend Snippet: DLS size distribution curves of the α-chymotrypsin (black), the P(DEAAm- co -GMA) copolymer (Sample C) (red) and the produced enzyme–polymer conjugate (blue).

    Techniques Used: Produced

    The relative activity of α-chymotrypsin (black) and the CT-P(DEAAm- co -GMA) enzyme–polymer nanoparticle (EPNP) (red) at 25 °C as a function of the time of thermal treatment at 45 °C.
    Figure Legend Snippet: The relative activity of α-chymotrypsin (black) and the CT-P(DEAAm- co -GMA) enzyme–polymer nanoparticle (EPNP) (red) at 25 °C as a function of the time of thermal treatment at 45 °C.

    Techniques Used: Activity Assay

    23) Product Images from "Reaction of fluorogenic reagents with proteins"

    Article Title: Reaction of fluorogenic reagents with proteins

    Journal:

    doi: 10.1016/j.chroma.2008.04.047

    Three protein standards labeled with Chromeo P465 and separated by A) CZE and B) CSE. 1.0 μM Ovalbumin (42.9 kDa), α-chymotrypsinogen A (25.7 kDa), and α-lactalbumin (14.2 kDa) were labeled with Chromeo P465 and diluted to 10 nM
    Figure Legend Snippet: Three protein standards labeled with Chromeo P465 and separated by A) CZE and B) CSE. 1.0 μM Ovalbumin (42.9 kDa), α-chymotrypsinogen A (25.7 kDa), and α-lactalbumin (14.2 kDa) were labeled with Chromeo P465 and diluted to 10 nM

    Techniques Used: Labeling

    24) Product Images from "Mechanisms of Enzymatic Degradation of Amyloid Beta Microfibrils Generating Nanofilaments and Nanospheres Related to Cytotoxicity †"

    Article Title: Mechanisms of Enzymatic Degradation of Amyloid Beta Microfibrils Generating Nanofilaments and Nanospheres Related to Cytotoxicity †

    Journal: Biochemistry

    doi: 10.1021/bi902134p

    CD analyses of the Aβ fibrils before and after enzymatic degradations for 24 h. Blue solid and dotted lines show the overall and filtrated Aβ fibrils solution before the enzymatic degradation. Green and orange solid and dotted lines show the overall and filtered Degradation Products (DP) by protease XIV and alpha-chymotrypsin, respectively.
    Figure Legend Snippet: CD analyses of the Aβ fibrils before and after enzymatic degradations for 24 h. Blue solid and dotted lines show the overall and filtrated Aβ fibrils solution before the enzymatic degradation. Green and orange solid and dotted lines show the overall and filtered Degradation Products (DP) by protease XIV and alpha-chymotrypsin, respectively.

    Techniques Used:

    Models of enzymatic reaction of Aβ fibrils in nano-meter scale by protease XIV and alpha-chymotrypsin. (A) Aβ with cross-beta structure, (B) spherical degradation products from protease XIV, and (C) nanofilaments from alpha-chymotrypsin.
    Figure Legend Snippet: Models of enzymatic reaction of Aβ fibrils in nano-meter scale by protease XIV and alpha-chymotrypsin. (A) Aβ with cross-beta structure, (B) spherical degradation products from protease XIV, and (C) nanofilaments from alpha-chymotrypsin.

    Techniques Used:

    Aβ fibrils after enzymatic degradation for 24h. AFM height images of Aβ fibrils during enzymatic degradation by protease XIV (A) and by alpha-chymotrypsin (B). (a) and (b) show line profile data of the crystals indicated by white lines in each figure.
    Figure Legend Snippet: Aβ fibrils after enzymatic degradation for 24h. AFM height images of Aβ fibrils during enzymatic degradation by protease XIV (A) and by alpha-chymotrypsin (B). (a) and (b) show line profile data of the crystals indicated by white lines in each figure.

    Techniques Used:

    Enzymatic digestion patterns of Aβ fibrils. MALDI-TOF analysis of Aβ fibrils before (A) and after the enzymatic degradation for 24 h by protease XIV (B) and alpha-chymotrypsin (C), for 48 h by NEP (D) and IDE (E).
    Figure Legend Snippet: Enzymatic digestion patterns of Aβ fibrils. MALDI-TOF analysis of Aβ fibrils before (A) and after the enzymatic degradation for 24 h by protease XIV (B) and alpha-chymotrypsin (C), for 48 h by NEP (D) and IDE (E).

    Techniques Used:

    Cell viability with the Aβ fibrils and their degradation fragments on differentiated PC-12 cells. Dependence of cell viability (percentage of active cells as compared to controls) on the Aβ peptides measured by MTS assay. Overall Aβ fibrils (blue open diamonds) show cell viability percentages of Aβ fibrils before the enzymatic degradation. Filtered soluble Aβ fragments (blue diamonds) shows cell viability percentages of filtered Aβ fibrils before the enzymatic degradation. Overall Degradation Products (DP) by protease XIV (orange squares) and alpha-chymotrypsin (green squares) show the percentages of each degradation products. Filtered soluble DP by protease XIV (orange open squares) and alpha-chymotrypsin (green open squares) show the percentages of each filtered degradation products. Data are represented as mean ± standard deviation ( n =8). *Significant difference between two groups at p
    Figure Legend Snippet: Cell viability with the Aβ fibrils and their degradation fragments on differentiated PC-12 cells. Dependence of cell viability (percentage of active cells as compared to controls) on the Aβ peptides measured by MTS assay. Overall Aβ fibrils (blue open diamonds) show cell viability percentages of Aβ fibrils before the enzymatic degradation. Filtered soluble Aβ fragments (blue diamonds) shows cell viability percentages of filtered Aβ fibrils before the enzymatic degradation. Overall Degradation Products (DP) by protease XIV (orange squares) and alpha-chymotrypsin (green squares) show the percentages of each degradation products. Filtered soluble DP by protease XIV (orange open squares) and alpha-chymotrypsin (green open squares) show the percentages of each filtered degradation products. Data are represented as mean ± standard deviation ( n =8). *Significant difference between two groups at p

    Techniques Used: MTS Assay, Standard Deviation

    25) Product Images from "A multifunctional surfactant catalyst inspired by hydrolases"

    Article Title: A multifunctional surfactant catalyst inspired by hydrolases

    Journal: Science Advances

    doi: 10.1126/sciadv.aaz0404

    An ACT. ( A ) The catalytic triad of active-site residues in α-chymotrypsin, highlighting the close proximity of each unit, facilitated by H-bonding ( 50 ). ( B ) A similarly close proximity of functional groups in the ACT surfactant is observed via single-crystal XRD, emphasizing the power of positioning active groups on a single, trifunctional molecule. ( C ) Assessment of the substrate carbonyl attack by the ACT surfactant (identified as rate-determining) via QM computation reveals a preferred pathway common to native enzymes, whereby the high-energy transition state is established by the nucleophilic ACT hydroxyl group.
    Figure Legend Snippet: An ACT. ( A ) The catalytic triad of active-site residues in α-chymotrypsin, highlighting the close proximity of each unit, facilitated by H-bonding ( 50 ). ( B ) A similarly close proximity of functional groups in the ACT surfactant is observed via single-crystal XRD, emphasizing the power of positioning active groups on a single, trifunctional molecule. ( C ) Assessment of the substrate carbonyl attack by the ACT surfactant (identified as rate-determining) via QM computation reveals a preferred pathway common to native enzymes, whereby the high-energy transition state is established by the nucleophilic ACT hydroxyl group.

    Techniques Used: Functional Assay

    A hydrolase-inspired cosurfactant catalyst. ( A ) Straightforward preparation of a novel surfactant incorporating an ACT of hydroxyl, carboxylate, and imidazole units as headgroup. ( B ) Self-assembly of the ACT surfactant with cosurfactants [hexadecyl guanidinium hydrochloride (Guan-C 16 ) and cetyltrimethylammonium bromide (CTAB)] yields a functionalized micelle with an internal hydrophobic core as a mimic of native hydrolase binding pockets. ( C ) The active site of a common hydrolase, α-chymotrypsin, highlighting a similar hydrophobic pocket and a catalytic triad of active residues to that of the ACT-surfactant system ( 74 ). ( D ) The ACT-surfactant coassembly displays an enhanced esterolytic effect for a model substrate when directly compared with the native enzyme α-chymotrypsin. (Data points are the mean of at least three independent experiments, and error bars represent SEM.)
    Figure Legend Snippet: A hydrolase-inspired cosurfactant catalyst. ( A ) Straightforward preparation of a novel surfactant incorporating an ACT of hydroxyl, carboxylate, and imidazole units as headgroup. ( B ) Self-assembly of the ACT surfactant with cosurfactants [hexadecyl guanidinium hydrochloride (Guan-C 16 ) and cetyltrimethylammonium bromide (CTAB)] yields a functionalized micelle with an internal hydrophobic core as a mimic of native hydrolase binding pockets. ( C ) The active site of a common hydrolase, α-chymotrypsin, highlighting a similar hydrophobic pocket and a catalytic triad of active residues to that of the ACT-surfactant system ( 74 ). ( D ) The ACT-surfactant coassembly displays an enhanced esterolytic effect for a model substrate when directly compared with the native enzyme α-chymotrypsin. (Data points are the mean of at least three independent experiments, and error bars represent SEM.)

    Techniques Used: Binding Assay

    26) Product Images from "Stability Studies of the Vaccine Adjuvant U-Omp19"

    Article Title: Stability Studies of the Vaccine Adjuvant U-Omp19

    Journal: Journal of Pharmaceutical Sciences

    doi: 10.1016/j.xphs.2020.10.011

    Impact of multiple freeze-thaw cycles on U-Omp19 stability. Samples of U-Omp19 were subjected to multiple freeze and thaw cycles. (a) SDS–PAGE Coomassie stained gels of non-reduced U-Omp19 samples after 0 (lane 2) to 6 (lane 8) freeze-thaw cycles. Lane 1: Molecular Weight Markers (MWM). (b) Percentage of α-chymotrypsin proteolytic activity remaining upon incubation with buffer (No inhibitor) or 50 μM of each U-Omp19 sample after 0 to 6 freeze-thaw cycles. (c) Dynamic light scattering measurements: Representative particle size distribution profiles by intensity and volume for U-Omp19 samples without freezing (Cycle 0) or after 1 or 6 freeze-thaw cycles.
    Figure Legend Snippet: Impact of multiple freeze-thaw cycles on U-Omp19 stability. Samples of U-Omp19 were subjected to multiple freeze and thaw cycles. (a) SDS–PAGE Coomassie stained gels of non-reduced U-Omp19 samples after 0 (lane 2) to 6 (lane 8) freeze-thaw cycles. Lane 1: Molecular Weight Markers (MWM). (b) Percentage of α-chymotrypsin proteolytic activity remaining upon incubation with buffer (No inhibitor) or 50 μM of each U-Omp19 sample after 0 to 6 freeze-thaw cycles. (c) Dynamic light scattering measurements: Representative particle size distribution profiles by intensity and volume for U-Omp19 samples without freezing (Cycle 0) or after 1 or 6 freeze-thaw cycles.

    Techniques Used: SDS Page, Staining, Molecular Weight, Activity Assay, Incubation

    Impact of lyophilization and long-term storage in solid state on protease inhibitor activity, protein integrity, and aggregation of U-Omp19. Samples of U-Omp19 were freeze dryed and placed for long term stability studies for up to 18 months at −80 °C, 4 °C, and 20 °C (RT). (a) Dynamic light scattering measurements: Comparison of particle size distribution profiles by intensity and volume for U-Omp19 samples without freeze drying (Control) or after lyophilization and instant reconstitution (t = 0). (b) SDS–PAGE Coomassie stained gel of reduced U-Omp19 samples. Lane 1: Molecular Weight Markers (MWM), Lane 2: U-Omp19 in aqueous solution (not lyophilized). Lane 3 to 5: lyophilized U-Omp19 after reconstitution stored in solid state for 18 months at the indicated temperatures. (c) Recovered inhibitor activity expressed as percentage of α-chymotrypsin proteolytic activity (mean ± SEM) remaining upon incubation with buffer (No inhibitor), 50 μM of U-Omp19 control sample (not lyophilized) or lyophilized and rehydrated U-Omp19 samples after storage in solid state for 18 months at indicated temperatures. ★★★: P
    Figure Legend Snippet: Impact of lyophilization and long-term storage in solid state on protease inhibitor activity, protein integrity, and aggregation of U-Omp19. Samples of U-Omp19 were freeze dryed and placed for long term stability studies for up to 18 months at −80 °C, 4 °C, and 20 °C (RT). (a) Dynamic light scattering measurements: Comparison of particle size distribution profiles by intensity and volume for U-Omp19 samples without freeze drying (Control) or after lyophilization and instant reconstitution (t = 0). (b) SDS–PAGE Coomassie stained gel of reduced U-Omp19 samples. Lane 1: Molecular Weight Markers (MWM), Lane 2: U-Omp19 in aqueous solution (not lyophilized). Lane 3 to 5: lyophilized U-Omp19 after reconstitution stored in solid state for 18 months at the indicated temperatures. (c) Recovered inhibitor activity expressed as percentage of α-chymotrypsin proteolytic activity (mean ± SEM) remaining upon incubation with buffer (No inhibitor), 50 μM of U-Omp19 control sample (not lyophilized) or lyophilized and rehydrated U-Omp19 samples after storage in solid state for 18 months at indicated temperatures. ★★★: P

    Techniques Used: Protease Inhibitor, Activity Assay, SDS Page, Staining, Molecular Weight, Incubation

    Impact of long-term storage on U-Omp19 protease inhibitor activity. Protease inhibitor activity was determined by an α-Chymotrypsin activity assay using a specific fluorogenic substrate in which the increment in fluorescence is proportional to proteolytic activity. α-Chymotrypsin was pre-incubated for 1 h with buffer (No inhibitor) or 50 μM of each U-Omp19 sample: fresh prepared (t = 0), or stored for different time periods (1 day or 1, 2, 3, 6, 9, 12, 18, 24 and 36 months) at the indicated temperatures (−80 °C, −20 °C, 4 °C, and 20 °C). Inhibitor activity is expressed as percentage of protease activity remaining when compared to “No inhibitor” condition (100% of activity). (a) Representative bar graph for the protease inhibitor activity analysis at time point = 36 months. Each bar represents the mean residual proteolytic activity of α-chymotrypsin and error bars represents SEM. ★★★: P
    Figure Legend Snippet: Impact of long-term storage on U-Omp19 protease inhibitor activity. Protease inhibitor activity was determined by an α-Chymotrypsin activity assay using a specific fluorogenic substrate in which the increment in fluorescence is proportional to proteolytic activity. α-Chymotrypsin was pre-incubated for 1 h with buffer (No inhibitor) or 50 μM of each U-Omp19 sample: fresh prepared (t = 0), or stored for different time periods (1 day or 1, 2, 3, 6, 9, 12, 18, 24 and 36 months) at the indicated temperatures (−80 °C, −20 °C, 4 °C, and 20 °C). Inhibitor activity is expressed as percentage of protease activity remaining when compared to “No inhibitor” condition (100% of activity). (a) Representative bar graph for the protease inhibitor activity analysis at time point = 36 months. Each bar represents the mean residual proteolytic activity of α-chymotrypsin and error bars represents SEM. ★★★: P

    Techniques Used: Protease Inhibitor, Activity Assay, Fluorescence, Incubation

    27) Product Images from "Proteolysis sensitizes LDL particles to phospholipolysis by secretory phospholipase A2 group V and secretory sphingomyelinase"

    Article Title: Proteolysis sensitizes LDL particles to phospholipolysis by secretory phospholipase A2 group V and secretory sphingomyelinase

    Journal: Journal of Lipid Research

    doi: 10.1194/jlr.M003103

    Effect of LDL fusion and size on phospholipolysis. LDL and IDL were first proteolyzed with α-chymotrypsin for 30 min, after which proteolysis was stopped by the addition of PMSF The proteolyzed LDL (panel A) and IDL (panel B) were incubated with
    Figure Legend Snippet: Effect of LDL fusion and size on phospholipolysis. LDL and IDL were first proteolyzed with α-chymotrypsin for 30 min, after which proteolysis was stopped by the addition of PMSF The proteolyzed LDL (panel A) and IDL (panel B) were incubated with

    Techniques Used: Incubation

    28) Product Images from "Highly stable trypsin-aggregate coatings on polymer nanofibers for repeated protein digestion"

    Article Title: Highly stable trypsin-aggregate coatings on polymer nanofibers for repeated protein digestion

    Journal: Proteomics

    doi: 10.1002/pmic.200800591

    Comparison of the enzyme stability of covalently-attached trypsin (CA-TR, filled circles) and trypsin-aggregate coatings (EC-TR, empty circles) in the presence of α-chymotrypsin.
    Figure Legend Snippet: Comparison of the enzyme stability of covalently-attached trypsin (CA-TR, filled circles) and trypsin-aggregate coatings (EC-TR, empty circles) in the presence of α-chymotrypsin.

    Techniques Used:

    29) Product Images from "Position-dependent impact of hexafluoroleucine and trifluoroisoleucine on protease digestion"

    Article Title: Position-dependent impact of hexafluoroleucine and trifluoroisoleucine on protease digestion

    Journal: Beilstein Journal of Organic Chemistry

    doi: 10.3762/bjoc.13.279

    Percentage of substrate remaining after incubation for 120 min (left) and 24 h (right) with α - chymotrypsin in 10 mM phosphate buffer, pH 7.4, at 30 °C. The data shown represent the average of three independent measurements. Errors are derived from the standard deviation.
    Figure Legend Snippet: Percentage of substrate remaining after incubation for 120 min (left) and 24 h (right) with α - chymotrypsin in 10 mM phosphate buffer, pH 7.4, at 30 °C. The data shown represent the average of three independent measurements. Errors are derived from the standard deviation.

    Techniques Used: Incubation, Derivative Assay, Standard Deviation

    Cleavage positions observed in the digestion of library peptides with α-chymotrypsin.
    Figure Legend Snippet: Cleavage positions observed in the digestion of library peptides with α-chymotrypsin.

    Techniques Used:

    30) Product Images from "Proteolysis sensitizes LDL particles to phospholipolysis by secretory phospholipase A2 group V and secretory sphingomyelinase"

    Article Title: Proteolysis sensitizes LDL particles to phospholipolysis by secretory phospholipase A2 group V and secretory sphingomyelinase

    Journal: Journal of Lipid Research

    doi: 10.1194/jlr.M003103

    Effect of LDL fusion and size on phospholipolysis. LDL and IDL were first proteolyzed with α-chymotrypsin for 30 min, after which proteolysis was stopped by the addition of PMSF The proteolyzed LDL (panel A) and IDL (panel B) were incubated with
    Figure Legend Snippet: Effect of LDL fusion and size on phospholipolysis. LDL and IDL were first proteolyzed with α-chymotrypsin for 30 min, after which proteolysis was stopped by the addition of PMSF The proteolyzed LDL (panel A) and IDL (panel B) were incubated with

    Techniques Used: Incubation

    31) Product Images from "Changes in solvent exposure reveal the kinetics and equilibria of adsorbed protein unfolding in hydrophobic interaction chromatography"

    Article Title: Changes in solvent exposure reveal the kinetics and equilibria of adsorbed protein unfolding in hydrophobic interaction chromatography

    Journal: Journal of chromatography. A

    doi: 10.1016/j.chroma.2010.06.051

    Isocratic elution chromatograms for (a) β-lactoglobulin B and (b) α-chymotrypsinogen A adsorbed to Butyl Sepharose ™  4 Fast Flow at various concentrations of ammonium sulfate.
    Figure Legend Snippet: Isocratic elution chromatograms for (a) β-lactoglobulin B and (b) α-chymotrypsinogen A adsorbed to Butyl Sepharose ™ 4 Fast Flow at various concentrations of ammonium sulfate.

    Techniques Used: Flow Cytometry

    Mass spectra of protein desorbed from Phenyl Sepharose ™  6 Fast Flow (high substitution) resin after labeling with deuterium for varied labeling times: (a) α-chymotrypsinogen A, 1.0 M ammonium sulfate; (b) β-lactoglobulin B, 0.8
    Figure Legend Snippet: Mass spectra of protein desorbed from Phenyl Sepharose ™ 6 Fast Flow (high substitution) resin after labeling with deuterium for varied labeling times: (a) α-chymotrypsinogen A, 1.0 M ammonium sulfate; (b) β-lactoglobulin B, 0.8

    Techniques Used: Flow Cytometry, Labeling

    Fractional labeling vs. labeling time for α-chymotrypsinogen A eluted from (a) Butyl Sepharose ™  4 Fast Flow and (b) Phenyl Sepharose ™  6 Fast Flow (high substitution) resins at ammonium sulfate concentrations of 0.8 M (squares),
    Figure Legend Snippet: Fractional labeling vs. labeling time for α-chymotrypsinogen A eluted from (a) Butyl Sepharose ™ 4 Fast Flow and (b) Phenyl Sepharose ™ 6 Fast Flow (high substitution) resins at ammonium sulfate concentrations of 0.8 M (squares),

    Techniques Used: Labeling, Flow Cytometry

    32) Product Images from "Highly-constrained bicyclic scaffolds for the discovery of protease-stable peptides via mRNA display"

    Article Title: Highly-constrained bicyclic scaffolds for the discovery of protease-stable peptides via mRNA display

    Journal: ACS chemical biology

    doi: 10.1021/acschembio.6b01006

    Protease stability a) Normalized protease degradation of each of the three scaffolded peptides shown to bind streptavidin with the highest affinity (7.2m, 9.4b, 9.5lin). 5 nM peptide was added to 1.4U of immobilized α-chymotrypsin. Aliquots were removed at the indicated time points and added directly to 1 μM streptavidin beads, incubated for 2h, and eluted with biotin. Peptides were quantified by scintillation of 35 S-cysteine labeled peptides and normalized to the no protease time point. Results are an average of duplicate trials.
    Figure Legend Snippet: Protease stability a) Normalized protease degradation of each of the three scaffolded peptides shown to bind streptavidin with the highest affinity (7.2m, 9.4b, 9.5lin). 5 nM peptide was added to 1.4U of immobilized α-chymotrypsin. Aliquots were removed at the indicated time points and added directly to 1 μM streptavidin beads, incubated for 2h, and eluted with biotin. Peptides were quantified by scintillation of 35 S-cysteine labeled peptides and normalized to the no protease time point. Results are an average of duplicate trials.

    Techniques Used: Incubation, Labeling

    33) Product Images from "Characterization of Novel Dipeptidyl Peptidase-IV Inhibitory Peptides from Soft-Shelled Turtle Yolk Hydrolysate Using Orthogonal Bioassay-Guided Fractionations Coupled with In Vitro and In Silico Study"

    Article Title: Characterization of Novel Dipeptidyl Peptidase-IV Inhibitory Peptides from Soft-Shelled Turtle Yolk Hydrolysate Using Orthogonal Bioassay-Guided Fractionations Coupled with In Vitro and In Silico Study

    Journal: Pharmaceuticals

    doi: 10.3390/ph13100308

    ( A ) DPP-IV inhibitory activity with soft shelled turtle yolk (SSTY) hydrolysates by trypsin, pepsin, α-chymotrypsin, and GI (pepsin, trypsin and α-chymotrypsin) enzyme, respectively. Different letters (a–f) indicate significant differences between samples ( p
    Figure Legend Snippet: ( A ) DPP-IV inhibitory activity with soft shelled turtle yolk (SSTY) hydrolysates by trypsin, pepsin, α-chymotrypsin, and GI (pepsin, trypsin and α-chymotrypsin) enzyme, respectively. Different letters (a–f) indicate significant differences between samples ( p

    Techniques Used: Activity Assay

    34) Product Images from "Cleavage of Type II Collagen by Cathepsin K in Human Osteoarthritic Cartilage"

    Article Title: Cleavage of Type II Collagen by Cathepsin K in Human Osteoarthritic Cartilage

    Journal: The American Journal of Pathology

    doi: 10.2353/ajpath.2008.070494

    C2C and C2K neoepitope contents in normal and OA articular cartilages. The cartilage was digested with α-chymotrypsin and C2C ( A ) and C2K ( B ) neoepitope levels were quantitated in the digests by competitive ELISAs. Nonarthritic cartilages were divided into two groups: N1 (patient ages, 15 to 38 years) and N2 (patient ages, 41 to 70 years); patient ages for OA cartilages ranged between 49 to 87 years. In both cases the difference between the median (bar) of neoepitope content in the nonarthritic and the OA cartilages was determined by Mann-Whitney analysis and the P values are shown in the figures.
    Figure Legend Snippet: C2C and C2K neoepitope contents in normal and OA articular cartilages. The cartilage was digested with α-chymotrypsin and C2C ( A ) and C2K ( B ) neoepitope levels were quantitated in the digests by competitive ELISAs. Nonarthritic cartilages were divided into two groups: N1 (patient ages, 15 to 38 years) and N2 (patient ages, 41 to 70 years); patient ages for OA cartilages ranged between 49 to 87 years. In both cases the difference between the median (bar) of neoepitope content in the nonarthritic and the OA cartilages was determined by Mann-Whitney analysis and the P values are shown in the figures.

    Techniques Used: MANN-WHITNEY

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    Size-exclusion Chromatography:

    Article Title: Bacteriophage Crosstalk: Coordination of Prophage Induction by Trans-Acting Antirepressors
    Article Snippet: .. Size-exclusion chromatography A Sephadex G75 column (Amersham) previously calibrated with α-chymotrypsin, ovalbumin and bovine serum albumin purchased from Sigma-Aldrich was connected to an Äkta P-9000 HPLC apparatus and a Frac-950 fraction collector. ..

    High Performance Liquid Chromatography:

    Article Title: Bacteriophage Crosstalk: Coordination of Prophage Induction by Trans-Acting Antirepressors
    Article Snippet: .. Size-exclusion chromatography A Sephadex G75 column (Amersham) previously calibrated with α-chymotrypsin, ovalbumin and bovine serum albumin purchased from Sigma-Aldrich was connected to an Äkta P-9000 HPLC apparatus and a Frac-950 fraction collector. ..

    Activated Clotting Time Assay:

    Article Title: EC-QCL mid-IR transmission spectroscopy for monitoring dynamic changes of protein secondary structure in aqueous solution on the example of β-aggregation in alcohol-denaturated α-chymotrypsin
    Article Snippet: Extended MCR-ALS was used to obtain pure spectral and concentration profiles of the temporal transition between α-helices and intermolecular β-sheets. .. Reagents and samples Sodium phosphate monobasic dihydrate p.a. (NaH2 PO4 •2H2 O) was purchased from Fluka (Buchs, Switzerland), sodium phosphate dibasic dihydrate (Na2 HPO4 •2H2 O) BioUltra, for molecular biology, sodium hydroxide solution 50 % in water (NaOH), hydrochloric acid 37 % (HCl) ACS reagent and 2,2,2-trifluoroethanol ReagentPlus ≥99 % (TFE), were obtained from Sigma-Aldrich (Steinheim, Germany). α-Chymotrypsin from bovine pancreas (≥85 %) (aCT) was obtained by Sigma-Aldrich (Steinheim, Germany) and used as purchased. .. Ultrapure water (18 MΩ cm) used for preparation of all solutions was obtained with a Milli-Q water purification system from Millipore (Bedford, USA).

    other:

    Article Title: Intracellular activation of ovastacin mediates pre-fertilization hardening of the zona pellucida
    Article Snippet: To measure the ZPH, ZP digestion using 2 mg/ml α-chymotrypsin (C4229, Sigma-Aldrich) in PBS (0.1% (w/v) PVA (polyvinylalcohol), 1 mM CaCl2 ) was performed as reported ( ).

    Activity Assay:

    Article Title: A novel dithiocarbamate analogue with potentially decreased ALDH inhibition has copper-dependent proteasome-inhibitory and apoptosis-inducing activity in human breast cancer cells
    Article Snippet: However, the accumulation of ubiquitinated proteins was detected by Western blot analysis in the cells treated with 9 -Cu and 1 -Cu but not in cells treated with 5 -Cu ( ). .. To further ascertain the proteasome-inhibitory activity of 9 -Cu, MDA-MB-231 cells were treated with 2.5 μM of 9 -Cu and 5 -Cu mixture for up to 24 h. We found that about 39% inhibition of the proteasomal chymotrypsin-like activity was achieved by 9 -Cu mixture after 2 h of treatment, 46% inhibition after 4 h, 65% inhibition after 8 h, 90% inhibition after 16 h. Proteasome inhibition was also confirmed by the accumulation of ubiquitinated proteins ( ). .. Since NOXA is ubiquitinated and degraded through the proteasome [ ], its expression can be an indirect marker of proteasome inhibition, thus we analyzed the expression of NOXA.

    Article Title: Defective Proteasome Delivery of Polyubiquitinated Proteins by Ubiquilin-2 Proteins Containing ALS Mutations
    Article Snippet: Cycloheximide-chase experiments The turnover of HA-tagged ubiquilin-2 and endogenous Myc protein was measured by immunoblotting equal amounts of protein lysate that were collected at various time intervals, as indicated in the figures, from HeLa cultures to which cycloheximide was added to a final concentration 100 μM to block new protein synthesis [ ]. .. Proteasome activity assays Proteasome activity (chymotrypsin-like activity) was measured using the 20S proteasome activity assay kit (Millipore), which uses N -succinyl-Leu-Leu-Val-Try-AMC (7-amino-4-methycoumarin) as a fluorogenic substrate. .. In these assays, equal amounts of protein contained in microsomes prepared from HEK293-CD3cells that were either mock transfected or transfected with siRNAs against erasin or ubiquilin-1/2 were incubated with the fluorogenic substrate with and without the proteasome inhibitor lactacystin [ ].

    Multiple Displacement Amplification:

    Article Title: A novel dithiocarbamate analogue with potentially decreased ALDH inhibition has copper-dependent proteasome-inhibitory and apoptosis-inducing activity in human breast cancer cells
    Article Snippet: However, the accumulation of ubiquitinated proteins was detected by Western blot analysis in the cells treated with 9 -Cu and 1 -Cu but not in cells treated with 5 -Cu ( ). .. To further ascertain the proteasome-inhibitory activity of 9 -Cu, MDA-MB-231 cells were treated with 2.5 μM of 9 -Cu and 5 -Cu mixture for up to 24 h. We found that about 39% inhibition of the proteasomal chymotrypsin-like activity was achieved by 9 -Cu mixture after 2 h of treatment, 46% inhibition after 4 h, 65% inhibition after 8 h, 90% inhibition after 16 h. Proteasome inhibition was also confirmed by the accumulation of ubiquitinated proteins ( ). .. Since NOXA is ubiquitinated and degraded through the proteasome [ ], its expression can be an indirect marker of proteasome inhibition, thus we analyzed the expression of NOXA.

    Inhibition:

    Article Title: A novel dithiocarbamate analogue with potentially decreased ALDH inhibition has copper-dependent proteasome-inhibitory and apoptosis-inducing activity in human breast cancer cells
    Article Snippet: However, the accumulation of ubiquitinated proteins was detected by Western blot analysis in the cells treated with 9 -Cu and 1 -Cu but not in cells treated with 5 -Cu ( ). .. To further ascertain the proteasome-inhibitory activity of 9 -Cu, MDA-MB-231 cells were treated with 2.5 μM of 9 -Cu and 5 -Cu mixture for up to 24 h. We found that about 39% inhibition of the proteasomal chymotrypsin-like activity was achieved by 9 -Cu mixture after 2 h of treatment, 46% inhibition after 4 h, 65% inhibition after 8 h, 90% inhibition after 16 h. Proteasome inhibition was also confirmed by the accumulation of ubiquitinated proteins ( ). .. Since NOXA is ubiquitinated and degraded through the proteasome [ ], its expression can be an indirect marker of proteasome inhibition, thus we analyzed the expression of NOXA.

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  • 99
    Millipore α chymotrypsin
    Gel exclusion chromatography of GfoR and GfoR∶GfoA complexes. Proteins were purified from strain MA8731 containing the GfoR plasmid pSEB11 as described in Materials and Methods . The strain was grown without (A) or with arabinose (B). About 10 µg of each protein preparation were applied to an Amersham Sephadex G75 column. 0.5 mL fractions were collected after the passage of the void volume, dried, resuspended in protein loading buffer and separated on a 12% SDS-polyacrylamide gel. Band identification was confirmed by anti-FLAG Western blotting (data not shown). The column was size-calibrated using <t>α-chymotrypsin,</t> ovalbumin and bovine serum albumin from Sigma-Aldrich.
    α Chymotrypsin, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/α chymotrypsin/product/Millipore
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    97
    Millipore tssp peptide chains
    PKC signals downstream upon <t>TsSP-MR</t> interaction. Quantification of flow cytometry analysis of the expression levels of ( a ) CCR2, ( b ) LFA-1 avidity and ( c ) LFA-1 affinity on human monocytes. These cells were cultured in the presence or absence of TsSP (40 μg/ml, 16 h), the PKC inhibitor Bisindolylmaleimide I (GF109203, 2 μM) and blocking antibodies for the MR or its isotype control (both 10 μg/ml). ( b ) and ( c ) are expressed as the percentage of avidity/affinity compared to total LFA-1. Cell supernatants were used to determine the levels of ( d ) <t>TNF-α</t> and ( e ) IL-10 secretion by enzyme-linked immunosorbent assay analysis. f PKC activation was determined by Western Blotting using phosphoPKC antibodies compared to GAPDH expression and images were subsequently quantified using ImageJ. Experiments were performed in triplicate using cells derived from 4 different human donors and the results are presented as the mean ( a-c ); the mean percentage ( d, e ) or the mean PKC phosphorylation +/− SEM. * p
    Tssp Peptide Chains, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Gel exclusion chromatography of GfoR and GfoR∶GfoA complexes. Proteins were purified from strain MA8731 containing the GfoR plasmid pSEB11 as described in Materials and Methods . The strain was grown without (A) or with arabinose (B). About 10 µg of each protein preparation were applied to an Amersham Sephadex G75 column. 0.5 mL fractions were collected after the passage of the void volume, dried, resuspended in protein loading buffer and separated on a 12% SDS-polyacrylamide gel. Band identification was confirmed by anti-FLAG Western blotting (data not shown). The column was size-calibrated using α-chymotrypsin, ovalbumin and bovine serum albumin from Sigma-Aldrich.

    Journal: PLoS Genetics

    Article Title: Bacteriophage Crosstalk: Coordination of Prophage Induction by Trans-Acting Antirepressors

    doi: 10.1371/journal.pgen.1002149

    Figure Lengend Snippet: Gel exclusion chromatography of GfoR and GfoR∶GfoA complexes. Proteins were purified from strain MA8731 containing the GfoR plasmid pSEB11 as described in Materials and Methods . The strain was grown without (A) or with arabinose (B). About 10 µg of each protein preparation were applied to an Amersham Sephadex G75 column. 0.5 mL fractions were collected after the passage of the void volume, dried, resuspended in protein loading buffer and separated on a 12% SDS-polyacrylamide gel. Band identification was confirmed by anti-FLAG Western blotting (data not shown). The column was size-calibrated using α-chymotrypsin, ovalbumin and bovine serum albumin from Sigma-Aldrich.

    Article Snippet: Size-exclusion chromatography A Sephadex G75 column (Amersham) previously calibrated with α-chymotrypsin, ovalbumin and bovine serum albumin purchased from Sigma-Aldrich was connected to an Äkta P-9000 HPLC apparatus and a Frac-950 fraction collector.

    Techniques: Chromatography, Purification, Plasmid Preparation, Western Blot

    PPIase activity of CypD in the mitochondrial matrix. Mitochondrial matrix (30 μg proteins) was preincubated in 100 mM NaCl, 50 mM HEPES/Tris (pH 8.0) at 25 °C for 15 min in the presence, where indicated, of 300 μM NADPH, 0.4 μM TrxR1, 3 μM Trx from E. coli or 1 μM auranofin (AF). PPIase activity was estimated by a coupled assay utilizing α-chymotrypsin as described under Methods. ( A ) time course of PPIase activity in different experimental conditions and ( B ) first-order rate constants (s -1 ) indicated in the ordinate axis (*p

    Journal: Scientific Reports

    Article Title: Mitochondrial Thioredoxin System as a Modulator of Cyclophilin D Redox State

    doi: 10.1038/srep23071

    Figure Lengend Snippet: PPIase activity of CypD in the mitochondrial matrix. Mitochondrial matrix (30 μg proteins) was preincubated in 100 mM NaCl, 50 mM HEPES/Tris (pH 8.0) at 25 °C for 15 min in the presence, where indicated, of 300 μM NADPH, 0.4 μM TrxR1, 3 μM Trx from E. coli or 1 μM auranofin (AF). PPIase activity was estimated by a coupled assay utilizing α-chymotrypsin as described under Methods. ( A ) time course of PPIase activity in different experimental conditions and ( B ) first-order rate constants (s -1 ) indicated in the ordinate axis (*p

    Article Snippet: The peptide N-succinyl-Ala-Ala-Pro-Phe-p -nitroanilide (Sigma-Aldrich, St. Louis, MO, USA) was dissolved (3 mM) in trifluoroethanol containing 470 mM LiCl, while 2.4 mM α-chymotrypsin (Sigma-Aldrich) was dissolved in 1 mM HCl.

    Techniques: Activity Assay

    Effect of ovastacin on zona pellucida hardening, ZP2 cleavage and fertilization rate ( A ) α-chymotrypsin zona pellucida (ZP) digestion of wild-type oocytes (+/+), ovastacin-deficient (−/−) oocytes and 2-cell embryos. ◦ = outlier; n : total oocytes. Addition of fetuin-B (2.5 μM), pefabloc (250 μM) and E64 (50 μM) was simultaneous to the activation of oocytes by Ca 2+ ionophore (2.5 μM). All experiments are statistically significant ( P

    Journal: Molecular Human Reproduction

    Article Title: Intracellular activation of ovastacin mediates pre-fertilization hardening of the zona pellucida

    doi: 10.1093/molehr/gax040

    Figure Lengend Snippet: Effect of ovastacin on zona pellucida hardening, ZP2 cleavage and fertilization rate ( A ) α-chymotrypsin zona pellucida (ZP) digestion of wild-type oocytes (+/+), ovastacin-deficient (−/−) oocytes and 2-cell embryos. ◦ = outlier; n : total oocytes. Addition of fetuin-B (2.5 μM), pefabloc (250 μM) and E64 (50 μM) was simultaneous to the activation of oocytes by Ca 2+ ionophore (2.5 μM). All experiments are statistically significant ( P

    Article Snippet: To measure the ZPH, ZP digestion using 2 mg/ml α-chymotrypsin (C4229, Sigma-Aldrich) in PBS (0.1% (w/v) PVA (polyvinylalcohol), 1 mM CaCl2 ) was performed as reported ( ).

    Techniques: Activation Assay

    PKC signals downstream upon TsSP-MR interaction. Quantification of flow cytometry analysis of the expression levels of ( a ) CCR2, ( b ) LFA-1 avidity and ( c ) LFA-1 affinity on human monocytes. These cells were cultured in the presence or absence of TsSP (40 μg/ml, 16 h), the PKC inhibitor Bisindolylmaleimide I (GF109203, 2 μM) and blocking antibodies for the MR or its isotype control (both 10 μg/ml). ( b ) and ( c ) are expressed as the percentage of avidity/affinity compared to total LFA-1. Cell supernatants were used to determine the levels of ( d ) TNF-α and ( e ) IL-10 secretion by enzyme-linked immunosorbent assay analysis. f PKC activation was determined by Western Blotting using phosphoPKC antibodies compared to GAPDH expression and images were subsequently quantified using ImageJ. Experiments were performed in triplicate using cells derived from 4 different human donors and the results are presented as the mean ( a-c ); the mean percentage ( d, e ) or the mean PKC phosphorylation +/− SEM. * p

    Journal: Acta Neuropathologica Communications

    Article Title: Trichuris suis induces human non-classical patrolling monocytes via the mannose receptor and PKC: implications for multiple sclerosis

    doi: 10.1186/s40478-015-0223-1

    Figure Lengend Snippet: PKC signals downstream upon TsSP-MR interaction. Quantification of flow cytometry analysis of the expression levels of ( a ) CCR2, ( b ) LFA-1 avidity and ( c ) LFA-1 affinity on human monocytes. These cells were cultured in the presence or absence of TsSP (40 μg/ml, 16 h), the PKC inhibitor Bisindolylmaleimide I (GF109203, 2 μM) and blocking antibodies for the MR or its isotype control (both 10 μg/ml). ( b ) and ( c ) are expressed as the percentage of avidity/affinity compared to total LFA-1. Cell supernatants were used to determine the levels of ( d ) TNF-α and ( e ) IL-10 secretion by enzyme-linked immunosorbent assay analysis. f PKC activation was determined by Western Blotting using phosphoPKC antibodies compared to GAPDH expression and images were subsequently quantified using ImageJ. Experiments were performed in triplicate using cells derived from 4 different human donors and the results are presented as the mean ( a-c ); the mean percentage ( d, e ) or the mean PKC phosphorylation +/− SEM. * p

    Article Snippet: Cleavage of TsSP peptide chains (using α-chymotrypsin (CT, Sigma, USA) and oxidation of glycan moieties (using sodium periodate (PI; 10 mM, Sigma) was performed as described previously [ ].

    Techniques: Flow Cytometry, Cytometry, Expressing, Cell Culture, Blocking Assay, Enzyme-linked Immunosorbent Assay, Activation Assay, Western Blot, Derivative Assay

    TsSP modulates monocytes via PKCδ signaling. Control or PKCδ-deficient human monocytes were treated with TsSP (40 μg/ml) after which ( a ) the patrolling cell phenotype was visualized by live cell imaging (10 h) and subsequently quantified by using Image J and the expression levels of ( b ) CCR2, ( c ) LFA-1 avidity and ( d ) LFA-1 affinity were analyzed and quantified using flow cytometry. Cell supernatants were used to determine the levels of ( e ) TNF-α and ( f ) IL-10 secretion by enzyme-linked immunosorbent assay analysis. Experiments were performed in triplicate using 3 human control donors ( a-f ) and 3 ( a-d ) or 2 ( e, f ) PKCδ-deficient donors and results are presented as the mean ( a, b ) or the mean percentage (C-F) +/− SEM. * p

    Journal: Acta Neuropathologica Communications

    Article Title: Trichuris suis induces human non-classical patrolling monocytes via the mannose receptor and PKC: implications for multiple sclerosis

    doi: 10.1186/s40478-015-0223-1

    Figure Lengend Snippet: TsSP modulates monocytes via PKCδ signaling. Control or PKCδ-deficient human monocytes were treated with TsSP (40 μg/ml) after which ( a ) the patrolling cell phenotype was visualized by live cell imaging (10 h) and subsequently quantified by using Image J and the expression levels of ( b ) CCR2, ( c ) LFA-1 avidity and ( d ) LFA-1 affinity were analyzed and quantified using flow cytometry. Cell supernatants were used to determine the levels of ( e ) TNF-α and ( f ) IL-10 secretion by enzyme-linked immunosorbent assay analysis. Experiments were performed in triplicate using 3 human control donors ( a-f ) and 3 ( a-d ) or 2 ( e, f ) PKCδ-deficient donors and results are presented as the mean ( a, b ) or the mean percentage (C-F) +/− SEM. * p

    Article Snippet: Cleavage of TsSP peptide chains (using α-chymotrypsin (CT, Sigma, USA) and oxidation of glycan moieties (using sodium periodate (PI; 10 mM, Sigma) was performed as described previously [ ].

    Techniques: Live Cell Imaging, Expressing, Flow Cytometry, Cytometry, Enzyme-linked Immunosorbent Assay

    TsSP-induced functional effects on monocytes are glycan-dependent. Primary human monocytes were treated with TsSP, periodate (PI)- or chymotrypsin (CT)-treated TsSP (all 40 μg/ml) after which the cell motility was instantly visualized by ( a ) live cell imaging (10 h) and subsequently quantified by using Image J. Monocytes that were incubated with TsSP or PI/CT-TsSP for 16 h were used to study ( b ) monocyte adhesion to brain endothelial cells as well as ( c ) monocyte transendothelial migration as studied by time-lapse video microscopy. These experiments were performed on control ( b ) or TNF-α-treated endothelial cells ( b and c ). Experiments were performed in triplicate using cells from 8 ( a ) or 5 ( b and c ) different human donors and the results are presented as the mean +/− SEM. * p

    Journal: Acta Neuropathologica Communications

    Article Title: Trichuris suis induces human non-classical patrolling monocytes via the mannose receptor and PKC: implications for multiple sclerosis

    doi: 10.1186/s40478-015-0223-1

    Figure Lengend Snippet: TsSP-induced functional effects on monocytes are glycan-dependent. Primary human monocytes were treated with TsSP, periodate (PI)- or chymotrypsin (CT)-treated TsSP (all 40 μg/ml) after which the cell motility was instantly visualized by ( a ) live cell imaging (10 h) and subsequently quantified by using Image J. Monocytes that were incubated with TsSP or PI/CT-TsSP for 16 h were used to study ( b ) monocyte adhesion to brain endothelial cells as well as ( c ) monocyte transendothelial migration as studied by time-lapse video microscopy. These experiments were performed on control ( b ) or TNF-α-treated endothelial cells ( b and c ). Experiments were performed in triplicate using cells from 8 ( a ) or 5 ( b and c ) different human donors and the results are presented as the mean +/− SEM. * p

    Article Snippet: Cleavage of TsSP peptide chains (using α-chymotrypsin (CT, Sigma, USA) and oxidation of glycan moieties (using sodium periodate (PI; 10 mM, Sigma) was performed as described previously [ ].

    Techniques: Functional Assay, Live Cell Imaging, Incubation, Migration, Microscopy