PTMScan ® Trypsin, Mass Spectrometry Grade

Trypsin digests polypeptides by hydrolysis at the carboxyl side of unmodified arginine and lysine residues (1). Proteolysis is slower when the cleavage site is flanked by acidic residues and will not occur if the lysine or arginine is followed by a proline (2-5). Trypsin's activity is optimal at pH 8.0 and is inhibited to varying degrees by organophosphorus compounds such as diisopropyl fluorophosphate, as well as EDTA, aprotinin, Ag+, and benzamidine (6-8). 1.Brown, W.E. and Wold, F. (1973) Biochemistry 12, 828-34. 2.Rodriguez, J. et al. (2008) J Proteome Res 7, 300-5. 3.Leiros, H.K. et al. (2004) Protein Sci 13, 1056-70. 4.Rawlings, N.D. and Barrett, A.J. (1994) Methods Enzymol 244, 19-61. 5.Perona, J.J. and Craik, C.S. (1995) Protein Sci 4, 337-60. 6.KOSTKA, V. and CARPENTER, F.H. (1964) J Biol Chem 239, 1799-803. 7.Levilliers, N. et al. (1970) Arch Biochem Biophys 140, 474-83. 8.Polgár, L. (2005) Cell Mol Life Sci 62, 2161-72.