Merck, SRP6509-100UG, Chymotrypsin from human pancreas

General description
Chymotrypsin from human pancreas 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. It is secreted by the pancreas as inactive chymotrypsinogen C. Molecular weight of this enzyme is found to be 25kDa. The pI is 8.75.
Biochem/physiol Actions
Chymotrypsin from human pancreas selectively hydrolyzes peptide bonds on the C-terminal side of tyrosine, phenylalanine, tryptophan and leucine. Loss-of-function mutations in this gene have been associated with increased risk of chronic pancreatitis. It has high activity toward leucyl peptide bonds. The enzyme acts as a co-activator of procarboxypeptidases A1 and A2.
Physical form
Lyophilized as a salt-free solid.