Abstract
Commercially available Tos-PheCH 2Cl-treated or untreated bovine trypsin (EC 3.4.21.4) is shown to catalyse minor tryptic hydrolysis at the carboxyl side of asparagine residues in globin chains. This activity is not removed by the purification of enzyme, using CM-cellulose chromatography and subsequent affinity chromatolography on trypsin inhibitor columns, neither is it inhibited by Tos-PheCh 2Cl treatment of the CM-cellulose purified enzyme. It is suggested that the ability to hydrolyse globin chains at asparagine residues may represent an inherent feature of the trypsin molecule.
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