α-Chymotrypsin from bovine pancreas (TLCK treated to inactivate residual tryspin activity), Type VII, essentially salt-free, lyophilized powder, ≥40 units/mg protein Sigma C3142
По запросу
- Производитель: Sigma
- Каталожный номер:
C3142 - CAS номер : 9004-07-3
Frequently Asked Questions
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Analysis Note
Protein determined by A
Biochem/physiol Actions
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.
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+.
Other Notes
View more information on chymotrypsin at www.sigma-aldrich.com/enz
Packaging
10, 25, 100 mg in glass bottle
Preparation Note
Derived from New Zealand-sourced pancreas.
TLCK treatment inactivates trypsin which may be present in chymotrypsin, without affecting the chymotrypsin activity.
Unit Definition
One unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C.
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.1
Характеристики реактива | |
storage temp. | −20°C |