Abstract
1. 1. Three distinct proteolytic components of Tenebrio molitor larvae are differentiated on the basis of selective inhibition by specific trypsin inhibitors: an endopeptidase—“ Tenebrio trypsin”—and two exopeptidases—carboxypeptidase B and amino-tripeptidase. 2. 2. The exo- and endopeptidase activities are separated by column chromatography on ECTEOLA-cellulose, Tenebrio trypsin eluting freely. The latter is further purified by absorption on CM-cellulose and subsequent gradient elution. 3. 3. Sulphydryl or chelating compounds activate, stabilize and partially reactivate the exopeptidase activity. 4. 4. The relative proteolytic and esterolytic activities of both bovine and Tenebrio trypsins are similar, and esterolysis of carbobenzoxy-tyrosine nitrophenyl ester is completely inhibited by “crystalline soybean trypsin inhibitor”; this is in contrast to chymotrypsin. The stages of enzymatic hydrolysis of polylysine are strikingly similar for both trypsins.
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