type
Type II
Quality Level
form
lyophilized powder
specific activity
≥40 units/mg protein
mol wt
25 kDa
composition
protein, ≥85%
color
white to off-white
UniProt accession no.
application(s)
diagnostic assay manufacturing
storage temp.
−20°C
Gene Information
cow ... CTRB1(618826)
Application
The enzyme from Sigma has been used to study the structure-function relationship in glycosylated α-chymotrypsin using immobilized metal-ion affinity chromatography (IMAC) and immobilized metal-ion affinity capillary electrophoresis (IMACE).
Biochem/physiol Actions
α-Chymotrypsin is a serine peptidase and has 241 amino acid residues contained in three polypeptide chains (A chain-13 residues, B chain-131 residues, and C chain-97 residues) linked by disulfide bridges. Molecular weight of this enzyme is found to be 25 kDa. The pI is 8.75. It selectively hydrolyzes peptide bonds on the C-terminal side of tyrosine, phenylalanine, tryptophan, and leucine. Ca2+ activates and stabilizes the enzyme. The enzyme is inhibited by diisopropyl fluorophosphate (DFP), phenylmethanesulfonyl fluoride (PMSF), N-p-tosyl-L-phenylalanine chloromethyl ketone (TPCK), chymostatin, aprotinin, α1-antitrypsin, and α2-macroglobulin, 10 mM Cu2+ and Hg2+.
A serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met, Leu) on the carboxyl end of the bond.
Preparation Note
Produced from 3× crystallized chymotrypsinogen
Analysis Note
Protein determined by E1%/280
Other Notes
One unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C.
View more information on chymotrypsin at www.sigma-aldrich.com/enzymeexplorer
signalword
Danger
Hazard Classifications
Acute Tox. 4 Oral - Aquatic Acute 1 - Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
저장 등급
11 - Combustible Solids
wgk
WGK 1
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
프로토콜
Follow our procedure for the determination of a chymotrypsin activity. This enzymatic assay of alpha chymotrypsin guides you through the entire process and necessary calculations.
문서
Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.
관련 콘텐츠
QC Methods
Antonio Jesús Vizcaíno et al.
Marine drugs, 18(6) (2020-06-24)
This piece of research evaluates the presence of protease inhibitors in the macroalga Ulva ohnoi and provides an initial overview of their mode of action. The ability of Ulva protease inhibitors to inhibit digestive proteases of three marine fish species
Ines Atuh Ngoh et al.
Experimental parasitology, 218, 107969-107969 (2020-08-29)
Invasion of human red blood cells (RBCs) by Plasmodium parasites is a crucial yet poorly characterised phenotype. Two-color flow cytometry (2cFCM) promises to be a very sensitive and high throughput method for phenotyping parasite invasion. However, current protocols require high
K Y Jiang et al.
Biochimica et biophysica acta, 1433(1-2), 198-209 (1999-08-14)
Chemical glycosylation of bovine alpha-chymotrypsin, by a glucosamine adduct on the carboxyl group, results in the modification of its catalytic activity. The structural alterations of alpha-chymotrypsin resulting from its glycosylation are studied by immobilized metal-ion affinity chromatography (IMAC) and immobilized


