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Vacuolar/Extravacuolar Distribution of Aminopeptidases in Giant Alga Chara australis and Partial Purification of One Such Enzyme.

Authors
Type
Published Article
Journal
PLANT PHYSIOLOGY
0032-0889
Publisher
American Society of Plant Biologists
Publication Date
Volume
84
Issue
3
Pages
720–725
Identifiers
PMID: 16665510
Source
Medline
License
Unknown

Abstract

The presence of two major aminopeptidases (aminopeptidases I and II) in the giant alga Chara australis was shown using polyacrylamide gel electrophoresis. Partially purified aminopeptidase I had a molecular weight of about 120,000, hydrolyzed both leucine-beta-naphthylamide (pH optimum 6.0) and alanine-beta-naphthylamide (pH optimum 7.5), and was located both inside and outside the vacuole. Aminopeptidase I was inhibited by p-chloromercuribenzoic acid, iodoacetic acid, 1,10-phenanthroline, and N-tosyl-l-phenylalanine chloromethyl ketone. Aminopeptidase II hydrolyzed alanine-beta-naphthylamide but not leucine-beta-naphthylamide and was located only outside the vacuole.

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