Plant Physiol. Illumina
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Plant Physiology 84:720-725 (1987)
© 1987 American Society of Plant Biologists

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Metabolism and Enzymology

Vacuolar/Extravacuolar Distribution of Aminopeptidases in Giant Alga Chara australis and Partial Purification of One Such Enzyme 1

Yuji Moriyasu, Katsuhiro Sakano2 and Masashi Tazawa

Department of Botany, Faculty of Science, University of Tokyo, Hongo, Tokyo 113, Japan

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.


2 Present address: National Institute of Agrobiological Resources, 2-1-2, Yatabe, Tsukuba, Ibaraki 305, Japan

1 Supported partly by Special Coordination Funds for the Promotion of Science and Technology from the Science and Technology Agency of Japan.







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