the description of Chymotrypsin

Chymotrypsin is a proteolytic enzyme,which preferentially catalyzes the hydrolysis of peptide bonds involving L-isomers of tyrosine, phenylalanine and tryptophan.The optimum pH is 8.0.The enzyme is inhibited by heavy metals, the natural trypsin inhibitors to various degrees.It is the zymogen form of chymotrypsin. It belongs to the molecular class of serine protease. The molecular weight of Chymotrypsinogen is 25000 Da.Chymotrypsinogen is purified by several crystallization stages, and shows a single band on SDS-PAGE.
Chymotrypsin is synthesized in the pancreas by protein biosynthesis as a precursor called chymotrypsinogen that is enzymatically inactive. On cleavage by trypsin into two parts that are still connected via an S-S bond, cleaved chymotrypsinogen molecules can activate each other by removing two small peptides in a trans-proteolysis. The resulting molecule is active chymotrypsin, a three-polypeptide molecule interconnected via disulfide bonds.
CAS:9004-07-3
Source:Bovine Pancreas
Storage:Preserve in tight containers,and avoid exposure to excessive heat.