C3142
α-Chymotrypsin from bovine pancreas
(TLCK treated to inactivate residual tryspin activity), Type VII, essentially salt-free, lyophilized powder, ≥40 units/mg protein
Sinónimos:
TLCK-Chymotrypsin
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Número CAS:
UNSPSC Code:
12352204
eCl@ss:
42010112
EC Number:
232-671-2
NACRES:
NA.54
MDL number:
Specific activity:
≥40 units/mg protein
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type
Type VII
form
essentially salt-free, lyophilized powder
specific activity
≥40 units/mg protein
mol wt
25 kDa
solubility
1 mM HCl: soluble 10 mg/mL, clear
UniProt accession no.
storage temp.
−20°C
Gene Information
cow ... CTRB1(618826)
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Application
α-Chymotrypsin from Sigma has been used to determine the crystal structures of two homologous inhibitors (pars intercerebralis major peptide-C and pars intercerebralis major peptide-D2v) from the insect Locusta migratoria by forming a complex with the enzyme.
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. Its 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, 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
TLCK treatment inactivates trypsin which may be present in chymotrypsin, without affecting the chymotrypsin activity.
Analysis Note
Protein determined by A1%/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
Clase de almacenamiento
11 - Combustible Solids
wgk
WGK 1
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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A Roussel et al.
The Journal of biological chemistry, 276(42), 38893-38898 (2001-08-10)
The crystal structures of two homologous inhibitors (PMP-C and PMP-D2v) from the insect Locusta migratoria have been determined in complex with bovine alpha-chymotrypsin at 2.1- and 3.0-A resolution, respectively. PMP-C is a potent bovine alpha-chymotrypsin inhibitor whereas native PMP-D2 is
Tobias Koschubs et al.
Nucleic acids research, 38(10), 3186-3195 (2010-02-04)
Mediator is the central coactivator complex required for regulated transcription by RNA polymerase (Pol) II. Mediator consists of 25 subunits arranged in the head, middle, tail and kinase modules. Structural and functional studies of Mediator are limited by the availability
Tommi Kotila et al.
Nature communications, 13(1), 3442-3442 (2022-06-16)
Actin polymerization generates forces for cellular processes throughout the eukaryotic kingdom, but our understanding of the 'ancient' actin turnover machineries is limited. We show that, despite > 1 billion years of evolution, pathogenic Leishmania major parasite and mammalian actins share the same
M Gestin et al.
Digestive diseases and sciences, 42(6), 1302-1311 (1997-06-01)
A specific method for pancreatic elastase II activity analysis was developed. True elastase II activity could be discriminated from that of elastase I and chymotrypsin. The postnatal development of four pancreatic proteases in the duodenal juice of children and in
Zhenyao Luo et al.
FEBS letters, 592(13), 2341-2350 (2018-06-02)
The bacterium Streptococcus pneumoniae (the pneumococcus) is a major human pathogen that requires Zn2+ for its survival and virulence in the host environment. Polyhistidine triad protein D (PhtD) has a known role in pneumococcal Zn2+ homeostasis. However, the mechanistic basis
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