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Merck
모든 사진(4)

주요 문서

C4879

Sigma-Aldrich

α-Chymotrypsinogen A from bovine pancreas

essentially salt-free, lyophilized powder

동의어(들):

chymotrypsin A zymogen

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About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC 코드:
12352204
NACRES:
NA.54

생물학적 소스

bovine pancreas

Quality Level

유형

Type II

형태

essentially salt-free, lyophilized powder

특이 활성도

≥40 units/mg solid

분자량

25,656 Da by calculation

정제법

6× crystallization

solubility

1 mM HCl: soluble 10 mg/mL, clear, colorless

UniProt 수납 번호

외래 활성

α-chymotrypsin ≤1 U/mg (prior to activation by trypsin)

저장 온도

−20°C

유전자 정보

일반 설명

Chymotrypsinogen from bovine pancreas is a zymogen containing 5 disulfide bridges. It has an isoelectric pH of 8.97.

애플리케이션

α-Chymotrypsinogen A from bovine pancreas has been used as model protein crystallization reproducibility studies. It has also been used in the hydrolysis of α-gliadins prior to mass spectroscopy studies.
The enzyme from Sigma has been used in the non-invasive determination of solid-state protein conformation using near infrared (NIR) spectroscopy. It has been used to study the partitioning of protein in polymer/polymer aqueous two-phase systems. The enzyme has also been used for self-interaction chromatography applications, to test the rapid measurement of protein osmotic second virial coefficients. In this technique, the protein is immobilized on chromatographic particles and its retention is measured using isocratic elution.

생화학적/생리학적 작용

Chymotrypsinogen A requires limited proteolysis for its activation. Chymotrypsinogen A may be activated by trypsin and chymotrypsin (autolytic activation) to form m α, β, γ, δ and π chymotrypsin (depending upon the conditions of activation). Chymotrypsin is a protease that will preferentially cleave peptides on the carboxyl side of aromatic amino acids including tryptophan, tyrosine, and phenylalanine. It will also hydrolyze peptides on the carboxyl side of leucine, methionine, and alanine.
A serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met) on the carboxyl end of the peptide bond.

단위 정의

After activation to Chymotrypsin, one unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C.

기타 정보

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

개인 보호 장비

Eyeshields, Gloves, type N95 (US)


시험 성적서(COA)

제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.

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문서 라이브러리 방문

On the activation of bovine chymotrypsinogen A. Conformational isomerization of alpha1-and kappa-chymotrypsin and their autolytic conversion to alpha-and gamma-chymotrypsin.
Sharma SK and Hopkins TR
The Journal of Biological Chemistry, 253(9), 3055-3061 (1978)
Structural basis of IgE binding to alpha-and gamma-gliadins: Contribution of disulfide bonds and repetitive and nonrepetitive domains
Mameri H, et al.
Journal of Agricultural and Food Chemistry, 63(29), 6546-6554 (2015)
9.1 Proteases: Facilitating a Difficult Reaction
Biochemistry (5th Edition) (2002)
Peter M Tessier et al.
Biophysical journal, 82(3), 1620-1631 (2002-02-28)
Weak protein interactions are often characterized in terms of the osmotic second virial coefficient (B(22)), which has been shown to correlate with protein phase behavior, such as crystallization. Traditional methods for measuring B(22), such as static light scattering, are too
Simulation of the activation of alpha-chymotrypsin: Analysis of the pathway and role of the propeptide
Matrai J, et al.
Protein Science, 13(12), 3139-3150 (2004)

문서

Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.

Chromatograms

application for HPLC

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