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

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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.