Aminopeptidases in Webbing Clothes Moth Larvae. Properties and Specificities of Enzymes of Highest Electrophoretic Mobility

Abstract

The group of aminopeptidase bands from Tineola bisselliella larvae with highest electrophoretic mobility in polyacrylamide gels were purified further and partially separated by ion exchange chromatography. Three aminopeptidase bands were present in this material and were very similar with respect to their pH optima (7· 7), their molecular weight of 94000, their responses to metal ions and enzyme inhibitors and in their substrate specificity requirements.