Vacuolar/Extravacuolar Distribution of Aminopeptidases in Giant Alga Chara australis and Partial Purification of One Such Enzyme
Author(s) -
Yuji Moriyasu,
Katsuhiro Sakano,
Masashi Tazawa
Publication year - 1987
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.84.3.720
Subject(s) - aminopeptidase , leucine , biochemistry , vacuole , biology , alanine , chara , enzyme , hydrolysis , polyacrylamide gel electrophoresis , amino acid , botany , cytoplasm
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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