α chymotrypsin  (Millipore)


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  • 99
    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
    a Time-dependent IR absorbance and b second-derivative spectra of 20 mg mL −1 <t>α-chymotrypsin</t> 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
    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
    https://www.bioz.com/result/α chymotrypsin/product/Millipore
    Average 99 stars, based on 148 article reviews
    Price from $9.99 to $1999.99
    α chymotrypsin - by Bioz Stars, 2020-11
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    Images

    1) 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

    2) 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

    3) Product Images from "Differential dehydration effects on globular proteins and intrinsically disordered proteins during film formation"

    Article Title: Differential dehydration effects on globular proteins and intrinsically disordered proteins during film formation

    Journal: Protein Science : A Publication of the Protein Society

    doi: 10.1002/pro.3118

    CD Spectra of Globular Soluble Proteins. CD spectra of soluble globular proteins representing the four CATH classes (mostly helical: panels A, B, and C; mostly sheet: panels D, E, and F; mixed helix/sheet: panels G and H; and irregular: panel I). Solid lines represent solution spectra, while dashed lines are from films. The error bars indicate one standard deviation in three repeated measurements. The proteins are A: hemoglobin, B: myoglobin, C: cytochrome C, D: α‐chymotrypsin, E: elastase, F: concanavalin A, G: ribonuclease A, H: carbonic anhydrase II, I: aprotinin.
    Figure Legend Snippet: CD Spectra of Globular Soluble Proteins. CD spectra of soluble globular proteins representing the four CATH classes (mostly helical: panels A, B, and C; mostly sheet: panels D, E, and F; mixed helix/sheet: panels G and H; and irregular: panel I). Solid lines represent solution spectra, while dashed lines are from films. The error bars indicate one standard deviation in three repeated measurements. The proteins are A: hemoglobin, B: myoglobin, C: cytochrome C, D: α‐chymotrypsin, E: elastase, F: concanavalin A, G: ribonuclease A, H: carbonic anhydrase II, I: aprotinin.

    Techniques Used: Standard Deviation

    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 "A possible role of neurotensin in NANC relaxation of longitudinal muscle of the jejunum and ileum of Wistar rats"

    Article Title: A possible role of neurotensin in NANC relaxation of longitudinal muscle of the jejunum and ileum of Wistar rats

    Journal: British Journal of Pharmacology

    doi: 10.1038/sj.bjp.0704914

    Effects of α-chymotrypsin on EFS-induced NANC relaxation of longitudinal muscle of the jejunum and ileum of Wistar rats
    Figure Legend Snippet: Effects of α-chymotrypsin on EFS-induced NANC relaxation of longitudinal muscle of the jejunum and ileum of Wistar rats

    Techniques Used:

    Effect of α-chymotrypsin on EFS-induced relaxation of longitudinal muscle in the jejunum of Wistar rats. When repetitive EFS at 10 Hz for 10 s led to reproducible relaxation, jejunal segments were treated with α-chymotrypsin (3 U ml −1 ) for 20 min. The relaxation after the treatment was compared to the control relaxation immediately before the treatment. The continuous line indicates the presence of α-chymotrypsin in the bathing fluid. After recording normal spontaneous movements, the chart was run at a fast speed immediately before the stimulation to make the relaxant response clear. Black bold lines indicate the duration of EFS for 10 s.
    Figure Legend Snippet: Effect of α-chymotrypsin on EFS-induced relaxation of longitudinal muscle in the jejunum of Wistar rats. When repetitive EFS at 10 Hz for 10 s led to reproducible relaxation, jejunal segments were treated with α-chymotrypsin (3 U ml −1 ) for 20 min. The relaxation after the treatment was compared to the control relaxation immediately before the treatment. The continuous line indicates the presence of α-chymotrypsin in the bathing fluid. After recording normal spontaneous movements, the chart was run at a fast speed immediately before the stimulation to make the relaxant response clear. Black bold lines indicate the duration of EFS for 10 s.

    Techniques Used:

    6) Product Images from "Probing the Conformation of the Fibronectin III1–2 Domain by Fluorescence Resonance Energy Transfer"

    Article Title: Probing the Conformation of the Fibronectin III1–2 Domain by Fluorescence Resonance Energy Transfer

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M805025200

    Effects of proteolysis on FRET in CIIIY. The fluorescence emission spectra of a 100 n m solution of proteins excited at 433 nm were collected between 460 and 540 nm in the absence and presence of 3.2 μg/ml of α-chymotrypsin. A , shown
    Figure Legend Snippet: Effects of proteolysis on FRET in CIIIY. The fluorescence emission spectra of a 100 n m solution of proteins excited at 433 nm were collected between 460 and 540 nm in the absence and presence of 3.2 μg/ml of α-chymotrypsin. A , shown

    Techniques Used: Fluorescence

    7) Product Images from "Solid state fluorescence of proteins in high throughput mode and its applications"

    Article Title: Solid state fluorescence of proteins in high throughput mode and its applications

    Journal: F1000Research

    doi: 10.12688/f1000research.2-82.v2

    Fluorescence emission spectra (AU, arbitrary units) of α-chymotrypsin. α-Chymotrypsin in aqueous buffer (10 mM Tris-HCl, pH 7.0) (black curve), lyophilized α-chymotrypsin powder (blue dashed curve) and solid sample of enzyme precipitated and rinsed with propanol (EPRP) of α-chymotrypsin (red curve). All these fluorescence emission spectra were recorded with excitation at 280 nm using excitation and emission slit widths of 2 nm and 5 nm, respectively.
    Figure Legend Snippet: Fluorescence emission spectra (AU, arbitrary units) of α-chymotrypsin. α-Chymotrypsin in aqueous buffer (10 mM Tris-HCl, pH 7.0) (black curve), lyophilized α-chymotrypsin powder (blue dashed curve) and solid sample of enzyme precipitated and rinsed with propanol (EPRP) of α-chymotrypsin (red curve). All these fluorescence emission spectra were recorded with excitation at 280 nm using excitation and emission slit widths of 2 nm and 5 nm, respectively.

    Techniques Used: Fluorescence

    8) Product Images from "Quantification of Multifunctional Dipeptide YA from Oyster Hydrolysate for Quality Control and Efficacy Evaluation"

    Article Title: Quantification of Multifunctional Dipeptide YA from Oyster Hydrolysate for Quality Control and Efficacy Evaluation

    Journal: BioMed Research International

    doi: 10.1155/2018/8437379

    YA content after treatment with pepsin, trypsin and  α -chymotrypsin, and carboxypeptidase A compared with that of control (without enzyme treatment). OH, oyster hydrolysate; PE, pepsin; TR, trypsin; CH,  α -chymotrypsin; CPA, carboxypeptidase A. The labels with different letters above each bar denote statistical significance ( p
    Figure Legend Snippet: YA content after treatment with pepsin, trypsin and α -chymotrypsin, and carboxypeptidase A compared with that of control (without enzyme treatment). OH, oyster hydrolysate; PE, pepsin; TR, trypsin; CH, α -chymotrypsin; CPA, carboxypeptidase A. The labels with different letters above each bar denote statistical significance ( p

    Techniques Used:

    9) Product Images from "Development of a Δ9-Tetrahydrocannabinol Amino Acid-Dicarboxylate Prodrug With Improved Ocular Bioavailability"

    Article Title: Development of a Δ9-Tetrahydrocannabinol Amino Acid-Dicarboxylate Prodrug With Improved Ocular Bioavailability

    Journal: Investigative Ophthalmology & Visual Science

    doi: 10.1167/iovs.16-20757

    IOP–Time profile for THC in normotensive and α-chymotrypsin–induced rabbit glaucoma model. Numbers in brackets represent concentration (%w/v) and dose (μg). Actual baseline values (mean ± SEM in mm Hg) for IOP in the different formulations: THC (0.5% w/v) in Tocrisolve (24.0 ± 2.2), THC (0.8% w/v) in Tocrisolve (24.5 ± 1.9), THC (0.8% w/v) in normotensive (normal) eyes (19.4 ± 0.3), and Tocrisolve (19.6 ± 1.4).
    Figure Legend Snippet: IOP–Time profile for THC in normotensive and α-chymotrypsin–induced rabbit glaucoma model. Numbers in brackets represent concentration (%w/v) and dose (μg). Actual baseline values (mean ± SEM in mm Hg) for IOP in the different formulations: THC (0.5% w/v) in Tocrisolve (24.0 ± 2.2), THC (0.8% w/v) in Tocrisolve (24.5 ± 1.9), THC (0.8% w/v) in normotensive (normal) eyes (19.4 ± 0.3), and Tocrisolve (19.6 ± 1.4).

    Techniques Used: Concentration Assay

    10) Product Images from "Clostridium sordellii Lethal Toxin Is Maintained in a Multimeric Protein Complex "

    Article Title: Clostridium sordellii Lethal Toxin Is Maintained in a Multimeric Protein Complex

    Journal: Infection and Immunity

    doi: 10.1128/IAI.72.6.3366-3372.2004

    Protease treatment of TcsL. TcsL (10 μg) was incubated with an excess of each indicated protease (15 μg) overnight prior to SDS-PAGE analysis. The pH value is indicated above the gel and each pH section follows this order of protease treatment: Lanes 2 and 7, TcsL; lanes 3 and 8, TcsL plus trypsin; lanes 4 and 9, TcsL plus α-chymotrypsin; lanes 5 and 10, TcsL plus V8 protease; and lanes 6 and 11, TcsL plus proteinase K. Lane 1 shows the molecular mass markers.
    Figure Legend Snippet: Protease treatment of TcsL. TcsL (10 μg) was incubated with an excess of each indicated protease (15 μg) overnight prior to SDS-PAGE analysis. The pH value is indicated above the gel and each pH section follows this order of protease treatment: Lanes 2 and 7, TcsL; lanes 3 and 8, TcsL plus trypsin; lanes 4 and 9, TcsL plus α-chymotrypsin; lanes 5 and 10, TcsL plus V8 protease; and lanes 6 and 11, TcsL plus proteinase K. Lane 1 shows the molecular mass markers.

    Techniques Used: Incubation, SDS Page

    11) 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

    12) 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

    13) Product Images from "M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils"

    Article Title: M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0191317

    YghJ M forms detergent- and protease-resistant aggregates. SDS-PAGE (A) and SDD-AGE (B) were used to visualize the YghJ M detergent-resistant aggregates. In both cases, two YghJ M samples were compared at the starting point (0 days) and after 2 weeks of incubation in non-denaturing conditions (14 days). The YghJ M samples at the initial point of incubation were incubated with 2% SDS at 20°C or boiled at 100°C. The YghJ M samples obtained at 14 days of incubation were incubated at temperature gradient from 20 to 100°C, as shown. The fractions of aggregates, oligomers, and monomers are indicated. A monoclonal anti-His 6 antibody was used. The positions of protein weight ladder bands are shown (kDa). (C) The sample of the YghJ M protein with concentration 1 mg/ml after 2 weeks of incubation in non-denaturing condition (see the “Experimental Procedures” section for details) was digested with α-chymotrypsin (Ct) at a 1:90 Ct-to-total protein mass ratio for 45 min at 20°C. After that reaction was terminated by addition of SDS-PAGE sample buffer. Then samples were immediately loaded onto the gel. Protein was detected by Western blotting with anti-His 6 antibodies. “U”–unboiled samples, “B’–samples were additionally boiled for 5 minutes at 100°C prior the loading onto the gel. “-“–samples without Ct, “+”–samples treated with Ct.
    Figure Legend Snippet: YghJ M forms detergent- and protease-resistant aggregates. SDS-PAGE (A) and SDD-AGE (B) were used to visualize the YghJ M detergent-resistant aggregates. In both cases, two YghJ M samples were compared at the starting point (0 days) and after 2 weeks of incubation in non-denaturing conditions (14 days). The YghJ M samples at the initial point of incubation were incubated with 2% SDS at 20°C or boiled at 100°C. The YghJ M samples obtained at 14 days of incubation were incubated at temperature gradient from 20 to 100°C, as shown. The fractions of aggregates, oligomers, and monomers are indicated. A monoclonal anti-His 6 antibody was used. The positions of protein weight ladder bands are shown (kDa). (C) The sample of the YghJ M protein with concentration 1 mg/ml after 2 weeks of incubation in non-denaturing condition (see the “Experimental Procedures” section for details) was digested with α-chymotrypsin (Ct) at a 1:90 Ct-to-total protein mass ratio for 45 min at 20°C. After that reaction was terminated by addition of SDS-PAGE sample buffer. Then samples were immediately loaded onto the gel. Protein was detected by Western blotting with anti-His 6 antibodies. “U”–unboiled samples, “B’–samples were additionally boiled for 5 minutes at 100°C prior the loading onto the gel. “-“–samples without Ct, “+”–samples treated with Ct.

    Techniques Used: SDS Page, Incubation, Protein Concentration, Western Blot

    14) Product Images from "A Novel 3-Dimensional Approach for Cardiac Regeneration"

    Article Title: A Novel 3-Dimensional Approach for Cardiac Regeneration

    Journal: Conference proceedings : ... Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE Engineering in Medicine and Biology Society. Annual Conference

    doi: 10.1109/EMBC.2015.7318714

    Release kinetics of α-chymotrypsin from 2% (continue lines) and 1% (dotted lines) alginate microspheres show an initial burst and variable cumulative release dependent upon CaCl 2 concentration of the gelling bath.
    Figure Legend Snippet: Release kinetics of α-chymotrypsin from 2% (continue lines) and 1% (dotted lines) alginate microspheres show an initial burst and variable cumulative release dependent upon CaCl 2 concentration of the gelling bath.

    Techniques Used: Concentration Assay

    15) Product Images from "A Model for the Stretch-Mediated Enzymatic Degradation of Silk Fibers"

    Article Title: A Model for the Stretch-Mediated Enzymatic Degradation of Silk Fibers

    Journal: Journal of the mechanical behavior of biomedical materials

    doi: 10.1016/j.jmbbm.2010.06.008

    Experimental data showing the degradation of a silk fiber during a 14 day exposure to α -chymotrypsin and to 60 daily loading-unloading cycles. Results shown are for the 30 th cycle on days 0 (top curve), 5, 7, 9, 12, and 14 (bottom curve). Overlapping
    Figure Legend Snippet: Experimental data showing the degradation of a silk fiber during a 14 day exposure to α -chymotrypsin and to 60 daily loading-unloading cycles. Results shown are for the 30 th cycle on days 0 (top curve), 5, 7, 9, 12, and 14 (bottom curve). Overlapping

    Techniques Used:

    16) Product Images from "Impact of Silk Biomaterial Structure on Proteolysis"

    Article Title: Impact of Silk Biomaterial Structure on Proteolysis

    Journal: Acta biomaterialia

    doi: 10.1016/j.actbio.2014.09.013

    Quantification of secondary structure in films and hydrogels after analysis by FT-IR. (A) β-sheet, (B) α-helix (C) random coil and (D) turns content after treatment with proteinase K, protease XIV, α-chymotrypsin, collagenase,
    Figure Legend Snippet: Quantification of secondary structure in films and hydrogels after analysis by FT-IR. (A) β-sheet, (B) α-helix (C) random coil and (D) turns content after treatment with proteinase K, protease XIV, α-chymotrypsin, collagenase,

    Techniques Used:

    SDS-PAGE of degradation products released from silk fibroin materials. (A) deionized water only, (B) proteinase K, (C) protease XIV, (D) α-chymotrypsin, and (E) collagenase. Days are listed as 1–5; control lanes are enzyme solution incubated
    Figure Legend Snippet: SDS-PAGE of degradation products released from silk fibroin materials. (A) deionized water only, (B) proteinase K, (C) protease XIV, (D) α-chymotrypsin, and (E) collagenase. Days are listed as 1–5; control lanes are enzyme solution incubated

    Techniques Used: SDS Page, Incubation

    Weight loss from enzymatic degradation of silk fibroin materials. Films (Figure 1A) and hydrogels (Figure 1B) were prepared from a 3% (w/v) silk fibroin solution and immersed in proteinase K, protease XIV, α-chymotrypsin, collagenase, MMP-1, MMP-2,
    Figure Legend Snippet: Weight loss from enzymatic degradation of silk fibroin materials. Films (Figure 1A) and hydrogels (Figure 1B) were prepared from a 3% (w/v) silk fibroin solution and immersed in proteinase K, protease XIV, α-chymotrypsin, collagenase, MMP-1, MMP-2,

    Techniques Used:

    17) 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:

    18) Product Images from "Binding Properties and Stability of the Ras-Association Domain of Rap1-GTP Interacting Adapter Molecule (RIAM)"

    Article Title: Binding Properties and Stability of the Ras-Association Domain of Rap1-GTP Interacting Adapter Molecule (RIAM)

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0031955

    Limited proteolysis, thermal stability and in-cell proteolysis assays indicate an unstable RA domain, but a stable RA-PH domain pair. ( A-D ) The limited proteolysis analysis of RIAM150-502 ( A ), RIAM1-261 ( B ), RIAM150-261 ( C ) and GST ( D ). Fragments that appeared upon α-chymotrypsin treatment are marked with arrows . The incubation times are included in the figure. ( E ) Temperature denaturation profiles of RIAM1-261 ( blue ), RIAM150-261 ( red ), RIAM 150-445 ( yellow ) and RIAM150-502 ( green ). ( F ) The profiles of Rap1B- Gpp(NH)p ( yellow ) and RIAM150-261 ( red ) in individual measurements and measured together ( green ). All measurements were repeated 5 times and the mean graph is shown. The fluorescence values are normalized in E and plotted as arbitrary units in F . ( G ) In vivo proteolysis assay of RIAM constructs in CHO cells. Tranfected myc-RIAM constructs after various cycloheximide treatment times (0 h, 2 h, 6 h) are labeled with anti-myc. In order to check the comparable sample amount, the samples were also labeled for α-tubulin. ( H ) The graph shows qualitatively the same changes to the myc-RIAM amount after cycloheximide treatment (mean ± SEM ( error bars ); n = 2).
    Figure Legend Snippet: Limited proteolysis, thermal stability and in-cell proteolysis assays indicate an unstable RA domain, but a stable RA-PH domain pair. ( A-D ) The limited proteolysis analysis of RIAM150-502 ( A ), RIAM1-261 ( B ), RIAM150-261 ( C ) and GST ( D ). Fragments that appeared upon α-chymotrypsin treatment are marked with arrows . The incubation times are included in the figure. ( E ) Temperature denaturation profiles of RIAM1-261 ( blue ), RIAM150-261 ( red ), RIAM 150-445 ( yellow ) and RIAM150-502 ( green ). ( F ) The profiles of Rap1B- Gpp(NH)p ( yellow ) and RIAM150-261 ( red ) in individual measurements and measured together ( green ). All measurements were repeated 5 times and the mean graph is shown. The fluorescence values are normalized in E and plotted as arbitrary units in F . ( G ) In vivo proteolysis assay of RIAM constructs in CHO cells. Tranfected myc-RIAM constructs after various cycloheximide treatment times (0 h, 2 h, 6 h) are labeled with anti-myc. In order to check the comparable sample amount, the samples were also labeled for α-tubulin. ( H ) The graph shows qualitatively the same changes to the myc-RIAM amount after cycloheximide treatment (mean ± SEM ( error bars ); n = 2).

    Techniques Used: Incubation, Fluorescence, In Vivo, Proteolysis Assay, Construct, Labeling

    19) 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

    20) Product Images from "?91, an Essential Subunit of Yeast Transcription Factor IIIC, Cooperates with ?138 in DNA Binding"

    Article Title: ?91, an Essential Subunit of Yeast Transcription Factor IIIC, Cooperates with ?138 in DNA Binding

    Journal: Molecular and Cellular Biology

    doi:

    TFC6 encodes a subunit of factor τ. DNA affinity-purified factor TFIIIC was complexed with the tRNA 3 Glu gene, and, when indicated, the complex was digested with 10 ng of α-chymotrypsin for 10 min at 25°C to generate the fast-migrating complex τB-tDNA. Complexes were then incubated with increasing amounts of polyclonal antibodies directed against τ91 for 45 min at 25°C. Protein-tDNA complexes were analyzed by electrophoresis. τ, position of τ-tDNA complexes; τ-IgG, band retarded upon antibody binding; τB, protease-resistant domain of TFIIIC bound to tDNA. Lanes 1 to 8, no protease; lanes 9 to 12, α-chymotrypsin treatment. Lane 1, no TFIIIC factor, lanes 2 and 9, no antibody, lanes 2 to 7 and 9 to 12, anti-τ91 immunoglobulin G (IgG). Lane 8, control mouse antibodies.
    Figure Legend Snippet: TFC6 encodes a subunit of factor τ. DNA affinity-purified factor TFIIIC was complexed with the tRNA 3 Glu gene, and, when indicated, the complex was digested with 10 ng of α-chymotrypsin for 10 min at 25°C to generate the fast-migrating complex τB-tDNA. Complexes were then incubated with increasing amounts of polyclonal antibodies directed against τ91 for 45 min at 25°C. Protein-tDNA complexes were analyzed by electrophoresis. τ, position of τ-tDNA complexes; τ-IgG, band retarded upon antibody binding; τB, protease-resistant domain of TFIIIC bound to tDNA. Lanes 1 to 8, no protease; lanes 9 to 12, α-chymotrypsin treatment. Lane 1, no TFIIIC factor, lanes 2 and 9, no antibody, lanes 2 to 7 and 9 to 12, anti-τ91 immunoglobulin G (IgG). Lane 8, control mouse antibodies.

    Techniques Used: Affinity Purification, Incubation, Electrophoresis, Binding Assay

    21) Product Images from "An Alternative Pin1 Binding and Isomerization Site in the N-Terminus Domain of PSD-95"

    Article Title: An Alternative Pin1 Binding and Isomerization Site in the N-Terminus Domain of PSD-95

    Journal: Frontiers in Molecular Neuroscience

    doi: 10.3389/fnmol.2020.00031

    Pin1 isomerizes full-length PSD-95. (A) A cis-trans isomerization scheme mediated by Pin1 on the succinyl-AEPY-p-nitronilide peptide. For representation, only EPY-p-nitronilide is shown. The predicted amounts of each isomer in solution (see “Materials and Methods/References” secton). The cis-trans isomerization assay to test the functionality of the purified GST-Pin1. (B) (Left) Table showing the experiment design for the α-chymotrypsin-coupled cis-trans isomerization assay. (Right) Scheme of the Pin1-mediated isomerization reaction, only N-terminus, PDZ1 and PDZ2 are shown. Input condition contains both cis and trans -N-terminus PSD-95, (−) PSD-95 product in the presence of α-chymotrypsin alone and (+) PSD-95 product in the presence of Pin1 with α-chymotrypsin. (C) Immunoblot showing the results of the in vitro α-chymotrypsin cis-trans isomerization of full-length PSD-95. Homogenates of COS cells expressing full-length PSD-95::EGFP were incubated with the isomerase dead GST-Pin RR68, 69AA or GST-Pin1 and treated with 0.1 μg of chymotrypsin. Reactions were subjected to Western immunoblotting with anti-PSD-95 and GST antibodies. (Middle) Quantification of immunoblot band intensities normalized to time 0 for the 135 kDa band ( n = 1).
    Figure Legend Snippet: Pin1 isomerizes full-length PSD-95. (A) A cis-trans isomerization scheme mediated by Pin1 on the succinyl-AEPY-p-nitronilide peptide. For representation, only EPY-p-nitronilide is shown. The predicted amounts of each isomer in solution (see “Materials and Methods/References” secton). The cis-trans isomerization assay to test the functionality of the purified GST-Pin1. (B) (Left) Table showing the experiment design for the α-chymotrypsin-coupled cis-trans isomerization assay. (Right) Scheme of the Pin1-mediated isomerization reaction, only N-terminus, PDZ1 and PDZ2 are shown. Input condition contains both cis and trans -N-terminus PSD-95, (−) PSD-95 product in the presence of α-chymotrypsin alone and (+) PSD-95 product in the presence of Pin1 with α-chymotrypsin. (C) Immunoblot showing the results of the in vitro α-chymotrypsin cis-trans isomerization of full-length PSD-95. Homogenates of COS cells expressing full-length PSD-95::EGFP were incubated with the isomerase dead GST-Pin RR68, 69AA or GST-Pin1 and treated with 0.1 μg of chymotrypsin. Reactions were subjected to Western immunoblotting with anti-PSD-95 and GST antibodies. (Middle) Quantification of immunoblot band intensities normalized to time 0 for the 135 kDa band ( n = 1).

    Techniques Used: Purification, In Vitro, Expressing, Incubation, Western Blot

    22) 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

    23) 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

    24) 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

    25) 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

    26) 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

    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 "Detection of protease activities by flash chronopotentiometry using a reversible polycation-sensitive polymeric membrane electrode"

    Article Title: Detection of protease activities by flash chronopotentiometry using a reversible polycation-sensitive polymeric membrane electrode

    Journal: Analytical biochemistry

    doi: 10.1016/j.ab.2011.04.036

    Flash chronopotentiometric responses to 100 µg/ml each of the peptides before addition of α-chymotrypsin (A) and after addition of 4 µl of 1-mg/ml α-chymotrypsin to 5 ml of the test solution (B). The numbers over the chronopotentiograms
    Figure Legend Snippet: Flash chronopotentiometric responses to 100 µg/ml each of the peptides before addition of α-chymotrypsin (A) and after addition of 4 µl of 1-mg/ml α-chymotrypsin to 5 ml of the test solution (B). The numbers over the chronopotentiograms

    Techniques Used:

    29) Product Images from "Tuning Chemical and Physical Crosslinks in Silk Electrogels for Morphological Analysis and Mechanical Reinforcement"

    Article Title: Tuning Chemical and Physical Crosslinks in Silk Electrogels for Morphological Analysis and Mechanical Reinforcement

    Journal: Biomacromolecules

    doi: 10.1021/bm4004892

    SEMs of the critical point dried silk hydrogels (a, c, e) before enzymatic degradation, and (b, d, f) after 3 days of the enzymatic degradation by α-chymotrypsin. The fibril structures were locally aligned in the electrogelled silk (a, b), and highly oriented in the vortex induced silk gels (c, d). No significant fiber alignment was observed in the spontaneously formed silk hydrogel (e, f).
    Figure Legend Snippet: SEMs of the critical point dried silk hydrogels (a, c, e) before enzymatic degradation, and (b, d, f) after 3 days of the enzymatic degradation by α-chymotrypsin. The fibril structures were locally aligned in the electrogelled silk (a, b), and highly oriented in the vortex induced silk gels (c, d). No significant fiber alignment was observed in the spontaneously formed silk hydrogel (e, f).

    Techniques Used:

    30) Product Images from "Phenotypic Modifications in Staphylococcus aureus Cells Exposed to High Concentrations of Vancomycin and Teicoplanin"

    Article Title: Phenotypic Modifications in Staphylococcus aureus Cells Exposed to High Concentrations of Vancomycin and Teicoplanin

    Journal: Frontiers in Microbiology

    doi: 10.3389/fmicb.2016.00013

    Activity of enzymes in S. aureus cells under no-stress conditions (Blank), following 8 h of exposure (A) to 100 mg/L of vancomycin (100 V) and teicoplanin (100 T), and following 5 h of post-antibiotic growth in fresh, drug-free MHB (B) . The maximum activity (100%) is referred to the maximum color intensity (5) suggested by the kit. The horizontal axis corresponds to the following enzymes: E2, alkaline phosphatase; E3, esterase (C4); E4, esterase lipase (C8); E5, lipase (C14); E6, leucine arylamidase; E7, valine arylamidase; E8, cystine arylamidase; E9, trypsin; E10, α-chymotrypsin; E11, acid phosphatase; E12, Naphtol-AS-BI-phosphohydrolase; E13, α-galactosidase; E14, β-galactosidase: E15, β-glucuronidase; E16, α-glucosidase; E17, β-glucosidase; E18, N -acetyl-β-glucosaminidase; E19, α-mannosidase; E20, α-fucosidase.
    Figure Legend Snippet: Activity of enzymes in S. aureus cells under no-stress conditions (Blank), following 8 h of exposure (A) to 100 mg/L of vancomycin (100 V) and teicoplanin (100 T), and following 5 h of post-antibiotic growth in fresh, drug-free MHB (B) . The maximum activity (100%) is referred to the maximum color intensity (5) suggested by the kit. The horizontal axis corresponds to the following enzymes: E2, alkaline phosphatase; E3, esterase (C4); E4, esterase lipase (C8); E5, lipase (C14); E6, leucine arylamidase; E7, valine arylamidase; E8, cystine arylamidase; E9, trypsin; E10, α-chymotrypsin; E11, acid phosphatase; E12, Naphtol-AS-BI-phosphohydrolase; E13, α-galactosidase; E14, β-galactosidase: E15, β-glucuronidase; E16, α-glucosidase; E17, β-glucosidase; E18, N -acetyl-β-glucosaminidase; E19, α-mannosidase; E20, α-fucosidase.

    Techniques Used: Activity Assay

    31) Product Images from "A potent and Kv1.3-selective analogue of the scorpion toxin HsTX1 as a potential therapeutic for autoimmune diseases"

    Article Title: A potent and Kv1.3-selective analogue of the scorpion toxin HsTX1 as a potential therapeutic for autoimmune diseases

    Journal: Scientific Reports

    doi: 10.1038/srep04509

    Stability of HsTX1[R14A]. Reversed-phase HPLC analysis after treatment with pepsin (A), α-chymotrypsin (B) and trypsin (C). (D) Haemolysis assay; comparison of the haemolytic ability of HsTX1 and its analogues to haemolysis induced by Triton X-100 indicates that neither HsTX1 nor its analogues induces significant haemolysis. Data shown as average ± SEM (N = 3).
    Figure Legend Snippet: Stability of HsTX1[R14A]. Reversed-phase HPLC analysis after treatment with pepsin (A), α-chymotrypsin (B) and trypsin (C). (D) Haemolysis assay; comparison of the haemolytic ability of HsTX1 and its analogues to haemolysis induced by Triton X-100 indicates that neither HsTX1 nor its analogues induces significant haemolysis. Data shown as average ± SEM (N = 3).

    Techniques Used: High Performance Liquid Chromatography, Haemolysis Assay

    32) 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

    33) Product Images from "Quantification of Multifunctional Dipeptide YA from Oyster Hydrolysate for Quality Control and Efficacy Evaluation"

    Article Title: Quantification of Multifunctional Dipeptide YA from Oyster Hydrolysate for Quality Control and Efficacy Evaluation

    Journal: BioMed Research International

    doi: 10.1155/2018/8437379

    YA content after treatment with pepsin, trypsin and  α -chymotrypsin, and carboxypeptidase A compared with that of control (without enzyme treatment). OH, oyster hydrolysate; PE, pepsin; TR, trypsin; CH,  α -chymotrypsin; CPA, carboxypeptidase A. The labels with different letters above each bar denote statistical significance ( p
    Figure Legend Snippet: YA content after treatment with pepsin, trypsin and α -chymotrypsin, and carboxypeptidase A compared with that of control (without enzyme treatment). OH, oyster hydrolysate; PE, pepsin; TR, trypsin; CH, α -chymotrypsin; CPA, carboxypeptidase A. The labels with different letters above each bar denote statistical significance ( p

    Techniques Used:

    34) 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:

    35) Product Images from "Human Enterovirus 71 Uncoating Captured at Atomic Resolution"

    Article Title: Human Enterovirus 71 Uncoating Captured at Atomic Resolution

    Journal: Journal of Virology

    doi: 10.1128/JVI.03029-13

    Purification of EV71 virions and characterization of the uncoating intermediate. (A) Purification of EV71 virions. The protein composition of the virion, which was purified as described in Materials and Methods, was determined using 15% SDS-PAGE analysis. Lane 1, molecular mass marker; lane 2, purified full virions. The calculated molecular masses of VP1, VP2, VP3, and VP4 are 32.6 kDa, 27.7 kDa, 26.4 kDa, and 7.5 kDa, respectively. The purified full virions contain all four structural proteins, i.e., VP1, VP2, VP3, and VP4. (B) Cryo-EM images of samples from the crystallization drops containing crystals of the uncoating intermediate (left) and purified naturally occurring empty particles (right). The internal density corresponded to the RNA genome in the uncoating intermediate, whereas the empty particle was completely devoid of internal density. The presence of the RNA genome inside the particle suggests that these are uncoating intermediates. (C) The uncoating intermediate is more protease sensitive than the full virion. The proteolytic sensitivities of the full virion and the uncoating intermediate were assessed by trypsin digestion as described in Materials and Methods. The digested samples were analyzed by Western blot using a VP1 antibody. Lane 1, hanging drops containing crystals of the uncoating intermediate. Lane 2, hanging drops containing crystals of the uncoating intermediate digested with trypsin for 1 h at 37°C. The truncated VP1 is indicated with an arrow. Lane 3, hanging drops containing crystals of the full virion. Lane 4, hanging drops containing crystals of the full virion digested with trypsin for 1 h at 37°C. VP1 in the full virion is resistant to trypsin digestion. (D) The VP4 in the uncoating intermediate is protected from α-chymotrypsin digestion. The uncoating intermediate was treated by α-chymotrypsin digestion as described in Materials and Methods. The digested samples were analyzed by Western blotting using a VP4 antibody, with VP2 as a loading control. Lane 1, hanging drops containing crystals of the uncoating intermediate were incubated at 25°C. Lane 2, hanging drops containing crystals of the uncoating intermediate were digested with α-chymotrypsin for 1 h at 25°C. The VP4 in the uncoating intermediate was resistant to protease digestion.
    Figure Legend Snippet: Purification of EV71 virions and characterization of the uncoating intermediate. (A) Purification of EV71 virions. The protein composition of the virion, which was purified as described in Materials and Methods, was determined using 15% SDS-PAGE analysis. Lane 1, molecular mass marker; lane 2, purified full virions. The calculated molecular masses of VP1, VP2, VP3, and VP4 are 32.6 kDa, 27.7 kDa, 26.4 kDa, and 7.5 kDa, respectively. The purified full virions contain all four structural proteins, i.e., VP1, VP2, VP3, and VP4. (B) Cryo-EM images of samples from the crystallization drops containing crystals of the uncoating intermediate (left) and purified naturally occurring empty particles (right). The internal density corresponded to the RNA genome in the uncoating intermediate, whereas the empty particle was completely devoid of internal density. The presence of the RNA genome inside the particle suggests that these are uncoating intermediates. (C) The uncoating intermediate is more protease sensitive than the full virion. The proteolytic sensitivities of the full virion and the uncoating intermediate were assessed by trypsin digestion as described in Materials and Methods. The digested samples were analyzed by Western blot using a VP1 antibody. Lane 1, hanging drops containing crystals of the uncoating intermediate. Lane 2, hanging drops containing crystals of the uncoating intermediate digested with trypsin for 1 h at 37°C. The truncated VP1 is indicated with an arrow. Lane 3, hanging drops containing crystals of the full virion. Lane 4, hanging drops containing crystals of the full virion digested with trypsin for 1 h at 37°C. VP1 in the full virion is resistant to trypsin digestion. (D) The VP4 in the uncoating intermediate is protected from α-chymotrypsin digestion. The uncoating intermediate was treated by α-chymotrypsin digestion as described in Materials and Methods. The digested samples were analyzed by Western blotting using a VP4 antibody, with VP2 as a loading control. Lane 1, hanging drops containing crystals of the uncoating intermediate were incubated at 25°C. Lane 2, hanging drops containing crystals of the uncoating intermediate were digested with α-chymotrypsin for 1 h at 25°C. The VP4 in the uncoating intermediate was resistant to protease digestion.

    Techniques Used: Purification, SDS Page, Marker, Crystallization Assay, Western Blot, Incubation

    36) 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

    37) Product Images from "Assembly of a Filamin Four-domain Fragment and the Influence of Splicing Variant-1 on the Structure *"

    Article Title: Assembly of a Filamin Four-domain Fragment and the Influence of Splicing Variant-1 on the Structure *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M110.195958

    Thermal stability and limited proteolysis assays of FLNa(18–21) and FLNa(18–21) var-1 support the unfolded nature of one domain. A , temperature denaturation profiles of FLNa(18–21) ( black ) and FLNa(18–21) var-1 ( red ) isoforms. B and C , limited proteolysis analysis of FLNa(18–21) ( B ) and FLNa(18–21) var-1 ( C ). Fragments that appeared upon α-chymotrypsin digestions are marked with arrows. D , schematic diagram of FLNa(18–21) var-1. The positions and approximate lengths of fragments formed in the limited proteolysis based on N-terminal sequencing analysis of FLNa(18–21) var-1 are marked.
    Figure Legend Snippet: Thermal stability and limited proteolysis assays of FLNa(18–21) and FLNa(18–21) var-1 support the unfolded nature of one domain. A , temperature denaturation profiles of FLNa(18–21) ( black ) and FLNa(18–21) var-1 ( red ) isoforms. B and C , limited proteolysis analysis of FLNa(18–21) ( B ) and FLNa(18–21) var-1 ( C ). Fragments that appeared upon α-chymotrypsin digestions are marked with arrows. D , schematic diagram of FLNa(18–21) var-1. The positions and approximate lengths of fragments formed in the limited proteolysis based on N-terminal sequencing analysis of FLNa(18–21) var-1 are marked.

    Techniques Used: Sequencing

    38) Product Images from "Production, structure and in vitro degradation of electrospun honeybee silk nanofibers"

    Article Title: Production, structure and in vitro degradation of electrospun honeybee silk nanofibers

    Journal: Acta Biomaterialia

    doi: 10.1016/j.actbio.2011.06.001

    Susceptibility of electrospun mats to α-chymotrypsin digestion. The percent of mat weight change determined from the increase in protein concentration in the digest solution (A). SDS-PAGE analysis of proteins present in the digest solution showing
    Figure Legend Snippet: Susceptibility of electrospun mats to α-chymotrypsin digestion. The percent of mat weight change determined from the increase in protein concentration in the digest solution (A). SDS-PAGE analysis of proteins present in the digest solution showing

    Techniques Used: Protein Concentration, SDS Page

    Bright field microscopy of electrospun honeybee silk mats. Mat before adding α-chymotrypsin (A), and same mat after 24 h incubation in α-chymotrypsin (B). Commassie Blue stained fragments of mat after α-chymotrypsin digestion (C).
    Figure Legend Snippet: Bright field microscopy of electrospun honeybee silk mats. Mat before adding α-chymotrypsin (A), and same mat after 24 h incubation in α-chymotrypsin (B). Commassie Blue stained fragments of mat after α-chymotrypsin digestion (C).

    Techniques Used: Microscopy, Incubation, Staining

    39) 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

    40) Product Images from "Design and development of stapled transmembrane peptides that disrupt the activity of G-protein–coupled receptor oligomers"

    Article Title: Design and development of stapled transmembrane peptides that disrupt the activity of G-protein–coupled receptor oligomers

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.RA119.009160

    Biophysical analysis of stapled peptides. A , amino acid sequence alignment of the targeted TM regions and disrupting peptides. Cys residues are in the reduced state. Blue bridges indicate the stapled amino acid residues. The HIV-TAT amino acid sequence is displayed in red . Yields, purity, and MALDI-TOF data are shown for the stapled peptides and negative control. B , CD analysis of 30–50 μ m peptides at 20 °C. For proteolytic stability studies, the peptide solution (55.5 μ m for trypsin and chymotrypsin and 11.1 μ m for serum) was incubated in the presence of 0.55 μg/ml trypsin from porcine pancreas ( E ), α-chymotrypsin ( F ), or mouse serum ( G ) at 37 °C for the indicated times (indicated on the x axis ). Data are mean ± S.E. ( error bars ) ( n = 3) percentage of intact peptide normalized to t = 0. Proteolytic half-lives and putative cleavage sites (predicted using the Expasy bioinformatics server's model with a 50% probability of cleavage) are indicated at the bottom of each panel . Positive correlation between helicity and half-life in trypsin/chymotrypsin ( C ) or serum ( D ) was determined by two-tailed Pearson's correlation test.
    Figure Legend Snippet: Biophysical analysis of stapled peptides. A , amino acid sequence alignment of the targeted TM regions and disrupting peptides. Cys residues are in the reduced state. Blue bridges indicate the stapled amino acid residues. The HIV-TAT amino acid sequence is displayed in red . Yields, purity, and MALDI-TOF data are shown for the stapled peptides and negative control. B , CD analysis of 30–50 μ m peptides at 20 °C. For proteolytic stability studies, the peptide solution (55.5 μ m for trypsin and chymotrypsin and 11.1 μ m for serum) was incubated in the presence of 0.55 μg/ml trypsin from porcine pancreas ( E ), α-chymotrypsin ( F ), or mouse serum ( G ) at 37 °C for the indicated times (indicated on the x axis ). Data are mean ± S.E. ( error bars ) ( n = 3) percentage of intact peptide normalized to t = 0. Proteolytic half-lives and putative cleavage sites (predicted using the Expasy bioinformatics server's model with a 50% probability of cleavage) are indicated at the bottom of each panel . Positive correlation between helicity and half-life in trypsin/chymotrypsin ( C ) or serum ( D ) was determined by two-tailed Pearson's correlation test.

    Techniques Used: Sequencing, Negative Control, Incubation, Two Tailed Test

    Related Articles

    High Performance Liquid Chromatography:

    Article Title: Chemical glycosylation of cytochrome c improves physical and chemical protein stability
    Article Snippet: .. Chemicals Cytochrome c from equine heart (EC 232-700-9), dextran from L. mesenteroides (EC 232–6775, average Mw = 9–11 kD), trypsin from porcine pancreas, α-chymotrypsin type II from bovine pancreas, caspase 3 substrate (DEVD-pNA), caspase 9 substrate (LEHD-pNa), disuccinimidyl suberate linker, protease inhibitor cocktail, 2,2’-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS), ammonium carbonate, dimethyl sulfoxide (DMSO), methylene chloride, acetone, and acetonitrile (HPLC grade) were from Sigma-Aldrich (St. Louis, MO). ..

    Fluorescence:

    Article Title: Pyropia yezoensis Protein Prevents Dexamethasone-Induced Myotube Atrophy in C2C12 Myotubes
    Article Snippet: .. 20S Proteasome Activity Assay The chymotrypsin-like activity of the 20S proteasome was measured by changes in the fluorescence of 7-amino-4-methylcoumarin (AMC) conjugated to the chymotrypsin peptide substrate LLVY, using a 20S proteasome activity assay kit (Chemicon, Temecula, CA, USA). .. In brief, cells were suspended in RIPA lysis buffer (50 mM Tris-HCl, pH 7.5, 150 mM sodium chloride, 0.5% sodium deoxycholate, 1% Triton X-100, 0.1% SDS, and 2 mM EDTA) containing protease inhibitors (1 mg/mL aprotinin, 1 mg/mL leupeptin, 1 mg/mL pepstatin A, 200 mM Na3 VO4 , 500 mM NaF, and 100 mM PMSF) and centrifuged at 16,000× g for 10 min at 4 °C.

    Protease Inhibitor:

    Article Title: Chemical glycosylation of cytochrome c improves physical and chemical protein stability
    Article Snippet: .. Chemicals Cytochrome c from equine heart (EC 232-700-9), dextran from L. mesenteroides (EC 232–6775, average Mw = 9–11 kD), trypsin from porcine pancreas, α-chymotrypsin type II from bovine pancreas, caspase 3 substrate (DEVD-pNA), caspase 9 substrate (LEHD-pNa), disuccinimidyl suberate linker, protease inhibitor cocktail, 2,2’-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS), ammonium carbonate, dimethyl sulfoxide (DMSO), methylene chloride, acetone, and acetonitrile (HPLC grade) were from Sigma-Aldrich (St. Louis, MO). ..

    Purification:

    Article Title: Changes in solvent exposure reveal the kinetics and equilibria of adsorbed protein unfolding in hydrophobic interaction chromatography
    Article Snippet: .. Bovine α-lactalbumin, bovine β-lactoglobulin B, and bovine α-chymotrypsinogen A were obtained from Sigma (St. Louis, MO, USA) and used without further purification. .. The HIC media used in this study were Phenyl Sepharose™ 6 Fast Flow (low substitution), Phenyl Sepharose™ 6 Fast Flow (high substitution) and Butyl Sepharose™ 4 Fast Flow bulk resins purchased from GE Healthcare (Piscataway, NJ, USA).

    other:

    Article Title: Prion Protein Paralog Doppel Protein Interacts with Alpha-2-Macroglobulin: A Plausible Mechanism for Doppel-Mediated Neurodegeneration
    Article Snippet: Proteins Apo-transferrin, mouse albumin, aprotinin and alpha-chymotrypsin were purchased from Sigma-Aldrich (St. Louis, MO, USA).

    Activity Assay:

    Article Title: Pyropia yezoensis Protein Prevents Dexamethasone-Induced Myotube Atrophy in C2C12 Myotubes
    Article Snippet: .. 20S Proteasome Activity Assay The chymotrypsin-like activity of the 20S proteasome was measured by changes in the fluorescence of 7-amino-4-methylcoumarin (AMC) conjugated to the chymotrypsin peptide substrate LLVY, using a 20S proteasome activity assay kit (Chemicon, Temecula, CA, USA). .. In brief, cells were suspended in RIPA lysis buffer (50 mM Tris-HCl, pH 7.5, 150 mM sodium chloride, 0.5% sodium deoxycholate, 1% Triton X-100, 0.1% SDS, and 2 mM EDTA) containing protease inhibitors (1 mg/mL aprotinin, 1 mg/mL leupeptin, 1 mg/mL pepstatin A, 200 mM Na3 VO4 , 500 mM NaF, and 100 mM PMSF) and centrifuged at 16,000× g for 10 min at 4 °C.

    Article Title: New Difluoro Knoevenagel Condensates of Curcumin, Their Schiff Bases and Copper Complexes as Proteasome Inhibitors and Apoptosis Inducers in Cancer Cells
    Article Snippet: .. Purified rabbit 20S proteasome and fluorogenic substrate Suc-LLVY-AMC for the proteasomal chymotrypsin-like (CT-like) activity were obtained from Calbiochem Inc. (San Diego, CA). ..

    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: .. 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).

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    Millipore α chymotrypsin fluorogenic substrate
    Quantitation of <t>α-chymotrypsin</t> activity in HeLa cell lysates. Cell lysates from cells treated or untreated with doxorubicin (1 μg/mL) were incubated with substrate 2 (100 μM) in reaction buffer (100 mM Tris pH 8, 10 mM CaCl 2 , 50
    α Chymotrypsin Fluorogenic Substrate, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 175 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Quantitation of α-chymotrypsin activity in HeLa cell lysates. Cell lysates from cells treated or untreated with doxorubicin (1 μg/mL) were incubated with substrate 2 (100 μM) in reaction buffer (100 mM Tris pH 8, 10 mM CaCl 2 , 50

    Journal: Analytical biochemistry

    Article Title: Development of inductively coupled plasma-mass spectrometry (ICP-MS) based protease assays

    doi: 10.1016/j.ab.2009.11.010

    Figure Lengend Snippet: Quantitation of α-chymotrypsin activity in HeLa cell lysates. Cell lysates from cells treated or untreated with doxorubicin (1 μg/mL) were incubated with substrate 2 (100 μM) in reaction buffer (100 mM Tris pH 8, 10 mM CaCl 2 , 50

    Article Snippet: Streptavidin Agarose bead suspension (binding capacity: > 85 nmol free biotin/mL) was purchased from EMD Biosciences. α-Chymotrypsin from bovine pancreas Type II was purchased from Sigma and was used without any further purification. α-Chymotrypsin fluorogenic substrate [Suc-AAPF-AMC] was purchased from EMD Biosciences.

    Techniques: Quantitation Assay, Activity Assay, Incubation

    Outline of the ICP-MS based protease assay. The protease substrate was digested with α-chymotrypsin. The undigested substrate was separated from the digestion product by adding streptavidin agarose bead suspension followed by centrifuging. The

    Journal: Analytical biochemistry

    Article Title: Development of inductively coupled plasma-mass spectrometry (ICP-MS) based protease assays

    doi: 10.1016/j.ab.2009.11.010

    Figure Lengend Snippet: Outline of the ICP-MS based protease assay. The protease substrate was digested with α-chymotrypsin. The undigested substrate was separated from the digestion product by adding streptavidin agarose bead suspension followed by centrifuging. The

    Article Snippet: Streptavidin Agarose bead suspension (binding capacity: > 85 nmol free biotin/mL) was purchased from EMD Biosciences. α-Chymotrypsin from bovine pancreas Type II was purchased from Sigma and was used without any further purification. α-Chymotrypsin fluorogenic substrate [Suc-AAPF-AMC] was purchased from EMD Biosciences.

    Techniques: Mass Spectrometry, Protease Assay

    α-Chymotrypsin cleavage of substrate 2. Substrate 2 (10 μM) was incubated with α-chymotrypsin 200 nM (◆) or 20 nM (◊) in reaction buffer (100 mM Tris pH 8, 10 mM CaCl 2 , 50 mM NaCl) at 25 °C. The reaction

    Journal: Analytical biochemistry

    Article Title: Development of inductively coupled plasma-mass spectrometry (ICP-MS) based protease assays

    doi: 10.1016/j.ab.2009.11.010

    Figure Lengend Snippet: α-Chymotrypsin cleavage of substrate 2. Substrate 2 (10 μM) was incubated with α-chymotrypsin 200 nM (◆) or 20 nM (◊) in reaction buffer (100 mM Tris pH 8, 10 mM CaCl 2 , 50 mM NaCl) at 25 °C. The reaction

    Article Snippet: Streptavidin Agarose bead suspension (binding capacity: > 85 nmol free biotin/mL) was purchased from EMD Biosciences. α-Chymotrypsin from bovine pancreas Type II was purchased from Sigma and was used without any further purification. α-Chymotrypsin fluorogenic substrate [Suc-AAPF-AMC] was purchased from EMD Biosciences.

    Techniques: Incubation

    Determination of the Michaelis constants for substrate 2 and α-chymotrypsin. Substrate 2 was incubated in reaction buffer (100 mM Tris pH 8, 10 mM CaCl 2 , 50 mM NaCl) with α-chymotrypsin (20 nM) for 5 minutes. The reaction was stopped by

    Journal: Analytical biochemistry

    Article Title: Development of inductively coupled plasma-mass spectrometry (ICP-MS) based protease assays

    doi: 10.1016/j.ab.2009.11.010

    Figure Lengend Snippet: Determination of the Michaelis constants for substrate 2 and α-chymotrypsin. Substrate 2 was incubated in reaction buffer (100 mM Tris pH 8, 10 mM CaCl 2 , 50 mM NaCl) with α-chymotrypsin (20 nM) for 5 minutes. The reaction was stopped by

    Article Snippet: Streptavidin Agarose bead suspension (binding capacity: > 85 nmol free biotin/mL) was purchased from EMD Biosciences. α-Chymotrypsin from bovine pancreas Type II was purchased from Sigma and was used without any further purification. α-Chymotrypsin fluorogenic substrate [Suc-AAPF-AMC] was purchased from EMD Biosciences.

    Techniques: Incubation

    Comparison of the detection of α-chymotrypsin activity using ICP-MS and fluorescence based assays. A) Substrate 2 (20 μM, ▲) or Suc-AAPF-AMC (20 μM, Δ) was incubated in reaction buffer (100 mM Tris pH 8, 10 mM CaCl

    Journal: Analytical biochemistry

    Article Title: Development of inductively coupled plasma-mass spectrometry (ICP-MS) based protease assays

    doi: 10.1016/j.ab.2009.11.010

    Figure Lengend Snippet: Comparison of the detection of α-chymotrypsin activity using ICP-MS and fluorescence based assays. A) Substrate 2 (20 μM, ▲) or Suc-AAPF-AMC (20 μM, Δ) was incubated in reaction buffer (100 mM Tris pH 8, 10 mM CaCl

    Article Snippet: Streptavidin Agarose bead suspension (binding capacity: > 85 nmol free biotin/mL) was purchased from EMD Biosciences. α-Chymotrypsin from bovine pancreas Type II was purchased from Sigma and was used without any further purification. α-Chymotrypsin fluorogenic substrate [Suc-AAPF-AMC] was purchased from EMD Biosciences.

    Techniques: Activity Assay, Mass Spectrometry, Fluorescence, Incubation

    Splenocytes exposed to Fnfs secrete IL-6 and TNF-alpha in a time- and dose-dependent fashion, indicating that Fnfs prepared by α -chymotrypsin digestion are biologically active. Murine splenocytes (1 × 10 6 ) were treated with heat-inactivated

    Journal:

    Article Title: Biologically Active Fibronectin Fragments Stimulate Release of MCP-1 and Catabolic Cytokines from Murine Retinal Pigment Epithelium

    doi: 10.1167/iovs.08-2495

    Figure Lengend Snippet: Splenocytes exposed to Fnfs secrete IL-6 and TNF-alpha in a time- and dose-dependent fashion, indicating that Fnfs prepared by α -chymotrypsin digestion are biologically active. Murine splenocytes (1 × 10 6 ) were treated with heat-inactivated

    Article Snippet: Purified fibronectin was digested overnight at 37°C with the following enzymes: 1 U/mL thrombin, 0.3 U/mL cathepsin-D, and 1 U/mL α -chymotrypsin (all from Calbiochem, La Jolla, CA).

    Techniques:

    Optimal enzymatic digestion of fibronectin, based on number of fragments, lasted 10 minutes with  α -chymotrypsin. Stained gels of electrophoresed Fnfs are depicted. After enzymatic digestion, protease inhibitor (pi) was added. ( A ) Murine serum

    Journal:

    Article Title: Biologically Active Fibronectin Fragments Stimulate Release of MCP-1 and Catabolic Cytokines from Murine Retinal Pigment Epithelium

    doi: 10.1167/iovs.08-2495

    Figure Lengend Snippet: Optimal enzymatic digestion of fibronectin, based on number of fragments, lasted 10 minutes with α -chymotrypsin. Stained gels of electrophoresed Fnfs are depicted. After enzymatic digestion, protease inhibitor (pi) was added. ( A ) Murine serum

    Article Snippet: Purified fibronectin was digested overnight at 37°C with the following enzymes: 1 U/mL thrombin, 0.3 U/mL cathepsin-D, and 1 U/mL α -chymotrypsin (all from Calbiochem, La Jolla, CA).

    Techniques: Staining, Protease Inhibitor