Purification and properties of an aminopeptidase from seeds of Japanese apricot.

Purification and properties of an aminopeptidase from seeds of Japanese apricot. Research Abstract Details 

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Purification and properties of an aminopeptidase from seeds of Japanese apricot. Abstract Text:

K Ninomiya,S Tanaka,S Kawata,S Makisumi,

An aminopeptidase was purified about 1,700-fold from seeds of Japanese apricot (Prunus mume Sieb.) by a seven-step procedure comprising extraction from seeds, ammonium sulfate fractionation, DEAE-cellulose chromatography, first and second DEAE-Sepharose chromatography, hydroxyapatite chromatography, and Sephadex G-200 gel filtration. The purified enzyme was shown to be homogeneous on polyacrylamide gel electrophoresis. The molecular weight of the enzyme was estimated to be about 56,000 by gel filtration on Sephadex G-200 and the isoelectric point was 4.9. The pH optimum for L-leucine beta-naphthylamide was between pH 6.5 and 7.0, and the enzyme was stable in the pH 5.0 to 8.3 region and up to 50 degrees C. The enzyme hydrolyzed a variety of aminopeptidase substrates with a free alpha-amino group. Of the amino acid beta-naphthylamides, the enzyme was highly specific for substrates with a hydrophobic side chain in the amino terminal residue. The enzyme was strongly inhibited by p-chloromercuribenzoate, heavy metals, diethyl pyrocarbonate, and photooxidation with methylene blue, but was not affected by thiol compounds, peptidase inhibitors of microbial origin, such as bestatin and puromycin, or metal chelating agents. No activation of the enzyme by metal ions was observed. These results suggest that the enzyme is a true aminopeptidase in which cysteine and histidine residues participate in the catalytic process, and is not classifiable as a metalloenzyme.

Purification and properties of an aminopeptidase from seeds of Japanese apricot. Publishing Authors By Initials

K Ninomiya,S Tanaka,S Kawata,S Makisumi,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research

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Purification and properties of an aminopeptidase from seeds of Japanese apricot. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 89

Page Numbers: 193-201

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jan

YEAR: 1981

Purification and properties of an aminopeptidase from seeds of Japanese apricot. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Purification and properties of an aminopeptidase from seeds of Japanese apricot. Keywords Mesh Terms:

KEYWORDS: Substrate Specificity

MESH TERMS: enzymology

Chemical & Substance for Abstract: Purification and properties of an aminopeptidase from seeds of Japanese apricot. Information

Substance Name: Aminopeptidases

Registry Number: EC 3.4.11.-

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Country: JAPAN

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MEDLINETA: J Biochem

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