Trypsin - Definition and Overview

Trypsin is a digestive enzyme that cleaves peptide bonds only at carboxyl side of lysine and arginine residiues. Aspartate (Asp 189) residue located in the catalytic pocket (S1) of trypsin is reponsible for attracting and stabilizing positively-charged lysine and/or arginine. The optimum pH for Trypsin is 8.

Many trypsin preparations contain some ... works in the small intestine, where it degrades proteins to polypeptides and amino acids.

Trypsin is often modified by TPCK, Tosyl Phenylalanyl Chloromethyl Ketone, which will inactivate chymotrypsin. This is important because in some applications, like MS, the specifity of cleavage is important.

Trypsin should be stored at very cold temperatures (between -20 and -5C) to prevent denaturation.