Properties of the major carboxypeptidase in the larvae of the webbing clothes moth, Tineola bisselliella

摘要: The larvae of the webbing clothes moth, Tineola bisselliella contain two carboxypeptidases (EC 3.4.12-) and one these has been purified by preparative polyacrylamide gel electrophoresis. Its pH optimum for hydrolysis N-benzyloxycarbonyl-glycyl-leucine was 7.5-7.7 its molecular weight as judged filtration 72 000. It is strongly inhibited disopropylfluorophosphate, thiol reagents some metal cations also 1:10 phenanthroline but not EDTA. Km V values 13 N-acyl dipeptides were determined. enzyme a strong preference neutral aliphatic amino acid residues does hydrolyse C-terminal proline, arginine or lysine. true carboxypeptidase, requiring an L-amino in position, with free carboxyl group hydrolysing peptide substrates consecutively from end. Dipeptides are cleaved much more slosly than tripeptides dipeptides.