Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an n-termial 6-amino acid leader sequence resulting in the 23.8kDa trypsin molecule. The
optimum pH is 8.0. Trypsin is inhibited by organophosphorus compounds such as diisopropylfluorophosphate and natural inhibitors from pancreas. Soybean, lima bean, and egg white are also source of natural inhibitors. Trypsin cleaves amide and ester bonds of Arg and Lys. The GenDEPOT’s Sequencing Grade Trypsin is treated with L-(tosylamido-2-phenyl) ethyl chloromethyl ketone to inhibit contaminating chymotryptic activity, chemically modified to promote stability and further purified to remove autolysis fragments, resulting in a highly stable trypsin product resistant to autolysis while retaining specificity.