α-Chymotrypsin from bovine pancreas Type II, lyophilized powder, ≥40 units/mg protein Sigma C4129
По запросу
- Производитель: Sigma
- Каталожный номер:
C4129 - CAS номер : 9004-07-3
Frequently Asked Questions
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Analysis Note
Protein determined by E
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. 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+.
Other Notes
View more information on chymotrypsin at www.sigma-aldrich.com/enz
Packaging
1, 10 g in poly bottle
250, 500 mg in poly bottle
Preparation Note
Derived from New Zealand-sourced pancreas
Produced from 3× crystallized chymotrypsinogen
Unit Definition
One unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C.
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).1
Характеристики реактива | |
storage temp. | −20°C |