Dec 1, 1975

Aminopeptidases in webbing clothes moth larvae. properties and specificities of enzymes of highest electrophoretic mobility

Australian Journal of Biological Sciences
C W Ward

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 94,000, their responses to metal ions and enzyme inhibitors and in their substrate specificity requirements. Kinetic constants were obtained for the hydrolysis of 17 different alpha-aminoacyl-beta-naphthylamides by these aminopeptidases, the most favoured substrates being the derivatives of alanine, methionine, proline, leucine, glycine, glutamic acid, lysine and arginine. The enzymes also hydrolyse amino acid amides, dipeptides, dipeptide amides, tripeptides and oligopeptides at the N-terminal end. These enzymes differ from the other aminopeptides in T. bisselliella in being able to hydrolyse bonds involving proline.

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Mentioned in this Paper

Enzyme Inhibitor Drugs
Naphthalenes
Tineola bisselliella
Derivatives
Amides
Polyacrylamide Gels
Enzymes, antithrombotic
Moths
Aminopeptidase
Proline

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