bovine α-chymotrypsin Search Results


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  • 99
    Worthington Biochemical tlck treated bovine α chymotrypsin
    Tlck Treated Bovine α Chymotrypsin, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 99/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/tlck treated bovine α chymotrypsin/product/Worthington Biochemical
    Average 99 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    tlck treated bovine α chymotrypsin - by Bioz Stars, 2020-10
    99/100 stars
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    99
    Millipore α chymotrypsin
    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
    α Chymotrypsin, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1349 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/α chymotrypsin/product/Millipore
    Average 99 stars, based on 1349 article reviews
    Price from $9.99 to $1999.99
    α chymotrypsin - by Bioz Stars, 2020-10
    99/100 stars
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    99
    Millipore bovine α chymotrypsin
    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.
    Bovine α Chymotrypsin, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 187 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bovine α chymotrypsin/product/Millipore
    Average 99 stars, based on 187 article reviews
    Price from $9.99 to $1999.99
    bovine α chymotrypsin - by Bioz Stars, 2020-10
    99/100 stars
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    91
    sarstedt bovine pancreas α chymotrypsin
    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.
    Bovine Pancreas α Chymotrypsin, supplied by sarstedt, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bovine pancreas α chymotrypsin/product/sarstedt
    Average 91 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    bovine pancreas α chymotrypsin - by Bioz Stars, 2020-10
    91/100 stars
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    89
    Valiant bovine α chymotrypsin
    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.
    Bovine α Chymotrypsin, supplied by Valiant, used in various techniques. Bioz Stars score: 89/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bovine α chymotrypsin/product/Valiant
    Average 89 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    bovine α chymotrypsin - by Bioz Stars, 2020-10
    89/100 stars
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    Image Search Results


    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

    Journal: BioMed Research International

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

    doi: 10.1155/2018/8437379

    Figure Lengend 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

    Article Snippet: Pepsin (Product No. P7000), trypsin (Product No. T9201), α -chymotrypsin (Product No. C7762), and carboxypeptidase A (Product No. SAE0046) were purchased from Sigma-Aldrich Corporation (Saint Louis, MO, USA).

    Techniques:

    Proteins identified by LC-MS/MS in circulating protein aggregates (CPA) enriched from ALS and HC pooled plasma samples and from aggregates enriched from brain. (A) Venn diagram showing CPA proteins unique to or shared by ALS and HC. (B) Venn diagram showing HC and ALS CPA proteins shared by brain aggregates. Five proteins were expressed in all 3 aggregate groups (actin cytoplasmic 1, tubulin alpha-4A chain isoform 2, clathrin heavy chain 1 isoform 2, collagen alpha-1(VI) and plectin isoform 7), while brain aggregates shared only one protein with ALS and HC CPA (cytoplasmic dynein 1 heavy chain 1 and collagen alpha-2(VI), respectively).

    Journal: bioRxiv

    Article Title: Analysis of circulating protein aggregates reveals pathological hallmarks of amyotrophic lateral sclerosis

    doi: 10.1101/2020.04.30.070979

    Figure Lengend Snippet: Proteins identified by LC-MS/MS in circulating protein aggregates (CPA) enriched from ALS and HC pooled plasma samples and from aggregates enriched from brain. (A) Venn diagram showing CPA proteins unique to or shared by ALS and HC. (B) Venn diagram showing HC and ALS CPA proteins shared by brain aggregates. Five proteins were expressed in all 3 aggregate groups (actin cytoplasmic 1, tubulin alpha-4A chain isoform 2, clathrin heavy chain 1 isoform 2, collagen alpha-1(VI) and plectin isoform 7), while brain aggregates shared only one protein with ALS and HC CPA (cytoplasmic dynein 1 heavy chain 1 and collagen alpha-2(VI), respectively).

    Article Snippet: Circulating and brain protein aggregates protease digestion Aggregates-enriched fractions were enzymatically digested using trypsin (V542A, Promega), α-Chymotrypsin (referred as Chymotrypsin in the text, C4129, Sigma), Calpain (208712, Millipore) and Enterokinase (11334115001, Roche).

    Techniques: Liquid Chromatography with Mass Spectroscopy

    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.

    Journal: Journal of chromatography. A

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

    doi: 10.1016/j.chroma.2010.06.051

    Figure Lengend 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.

    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.

    Techniques: 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

    Journal: Journal of chromatography. A

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

    doi: 10.1016/j.chroma.2010.06.051

    Figure Lengend 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

    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.

    Techniques: 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),

    Journal: Journal of chromatography. A

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

    doi: 10.1016/j.chroma.2010.06.051

    Figure Lengend 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),

    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.

    Techniques: Labeling, Flow Cytometry