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Moriyasu Y, Miyoshi Y. Partial Purification and Characterization of Aminopeptidase II from Chara australis. Plant Physiol. 1989;89(2):687-91doi: 10.1104/pp.89.2.687.
Moriyasu, Y., & Miyoshi, Y. (1989). Partial Purification and Characterization of Aminopeptidase II from Chara australis. Plant physiology, 89(2), 687-91. https://doi.org/10.1104/pp.89.2.687
Moriyasu, Y, and Miyoshi, Y. "Partial Purification and Characterization of Aminopeptidase II from Chara australis." Plant physiology vol. 89,2 (1989): 687-91. doi: https://doi.org/10.1104/pp.89.2.687
Moriyasu Y, Miyoshi Y. Partial Purification and Characterization of Aminopeptidase II from Chara australis. Plant Physiol. 1989 Feb;89(2):687-91. doi: 10.1104/pp.89.2.687. PMID: 16666602; PMCID: PMC1055902.
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Plant Physiol. 1989 Feb;89(2):687-91. doi: 10.1104/pp.89.2.687.

Partial Purification and Characterization of Aminopeptidase II from Chara australis.

Plant physiology

Y Moriyasu, Y Miyoshi

Affiliations

  1. Department of Biology, University of Shizuoka, Yada 395, Shizuoka 422, Japan.

PMID: 16666602 PMCID: PMC1055902 DOI: 10.1104/pp.89.2.687

Abstract

Aminopeptidase II, one of the two major aminopeptidases in the giant alga Chara australis, was partially purified. Its molecular weight was estimated to be about 80,000 by gel permeation chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis showed that it is composed of a single polypeptide with a molecular weight of about 85,000. Aminopeptidase II hydrolyzed alanine-2-naphthylamide more efficiently than the naphthylamides of lysine and proline, and only weakly hydrolyzed the naphthylamides of arginine, phenylalanine, valine, and leucine. The optimal pH for the hydrolysis of alanine-2-naphthylamide was near 7.0. The activity of aminopeptidase II was inhibited by the SH-reagents p-chloromercuribenzoic acid and N-ethylmaleimide and by the metal chelator 1,10-phenanthroline.

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