Trypsin is a single chain polypeptide of 223 amino acid residues and is a member of the serine protease family. The active site amino acid residues of trypsin include HIs46 and Ser183. Trypsin is produced by removing the N-terminal hexapeptide from trypsinogen which is cleaved at the peptide bonds at Lys6 - lle7. This cleavage yields a single chain native form of trypsin called β-Trypsin. Ensuing autolysis of β-Trypsin results in α-Trypsin having two peptide chains bound by disulphide bonds. This enzyme predominantly cleaves peptide chains at the carboxyl side of Arginine and Lysine, with an exception when either one is followed by a Proline.
Form: Powder stabilized with lactose.
Activity: ≥ 250,000 USP units/gm
Chymotrypsin: ≥ 75,000 USP units/gm.
Unit Definition: One unit causes a change in absorbance of 0.003/min with BAEE as a substrate at 25°C, pH 7.6.