Frequently Asked Questions

Frequently Asked Questions are available for this Product.

Analysis Note

由 A 1%/280 测定的蛋白质

Biochem/physiol Actions

一种丝氨酸蛋白酶，能将与芳香烃或其他大型疏水性侧链（Tyr、Trp、Phe、Met、Leu）结合的肽从键的羧基端水解。

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/enzymeexplorer

包装

10, 25, 100 mg in glass bottle

Preparation Note

TLCK treatment inactivates trypsin which may be present in chymotrypsin, without affecting the chymotrypsin activity.

来源于新西兰产地的胰脏。

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.