α-Chymotrypsin preferentially catalyzes the hydrolysis of peptide bonds involving L-isomers of tyrosine, phenylalanine, and tryptophan. It also readily acts upon amides and esters of susceptible amino acids. In addition to bonds involving aromatic amino acids, chymotrypsin catalyzes at a high rate the hydrolysis of bonds of leucyl, methionyl, asparaginyl, and glutamyl residues.
A pancreas extract contains equal amounts of two forms of the zymogen: Chymotrypsinogen A, with a molecular weight of 25,000 and and isoelectric point of 9.1, and Chymotrypsinogen B (E.C.3.4.4.6), with an isoelectric point of 5.2. Together, the zymogens represent 32% of the protein content of pancreatic extracts. Dependent upon the conditions, chymotrypsinogen A may be activated to α-, π-, δ-, β-, or γ -chymotrypsin.
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.
Specific Activity: ~35 u/mg protein
Product Type: Biochemicals
Gene Id: cow ... CTRB1(618826)
Extinction Coefficient (E1%): 20.4. (Lit.)
Presentation: White Powder
Format: Powder
NOTES:
Inhibitors: The enzyme is inhibited by heavy metals, the natural trypsin inhibitors to various degrees, an inhibitor from potato, and organophosphorus compounds. Gel filtration of chymotrypsin removes autolysis products and other contaminants. The specificity of α-chloroketone as α-chymotrypsin inhibitor has been studied. It has been reported that phenothiazine-N-carbonyl chloride are specific for chymotrypsin inhibition. Also inhibited by AEBSF, α-1-antitrypsin, Aprotinin, DFP, PMSF, TPCK and α-2-Macroglobulin.
Storage & Handling: Store at +4°C.