Purification and properties of a proline iminopeptidase from apricot seeds.

Purification and properties of a proline iminopeptidase from apricot seeds. Research Abstract Details 

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Purification and properties of a proline iminopeptidase from apricot seeds. Abstract Text:

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

A proline iminopeptidase was purified about 18,000-fold from apricot seeds (Prunus armeniaca LINN.) by a five-step procedure comprised of extraction from seeds, ammonium sulfate fractionation, DEAE-cellulose chromatography, CM-Sepharose chromatography, and rechromatography on CM-Sepharose. The purified enzyme had a molecular weight of 220,000 by gel filtration and 55,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This indicates that the native enzyme may be composed of four identical subunits. The isoelectric point was 6.2 as determined by gel electrofocusing. The pH optimum for L-proline beta-naphthylamide was between pH 7.5 and 8.0, and the enzyme was stable in the pH 6.5-to-8.0 region and up to 40 degrees C. The enzyme was specific for L-proline beta-naphthylamide among various amino acid beta-naphthylamides, and it also hydrolzyed L-prolylglycine and L-prolylglycylglycine. The enzyme was strongly inhibited by p-chloromercuribenzoate, 5,5'-dithiobis(2-nitrobenzoic acid), N-ethylmaleimide, and heavy metal ions, but was not activated significantly by thiol compounds. Moreover, the enzyme was inactivated by diethyl pyrocarbonate, p-bromophenacyl bromide, and photooxidation, but was not affected by diisopropyl fluorophosphate, phenylmethanesulfonyl fluoride, bestatin, puromycin, or metal chelating agents. No activation of the enzyme was observed on addition of metal ions. These results suggest that the enzyme is not classifiable as a metalloenzyme, and that cysteine and histidine residues may participate in the enzyme activity.

Purification and properties of a proline iminopeptidase from apricot seeds. Publishing Authors By Initials

K Ninomiya,K Kawatani,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 a proline iminopeptidase from apricot seeds. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 92

Page Numbers: 413-21

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Aug

YEAR: 1982

Purification and properties of a proline iminopeptidase from apricot seeds. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Purification and properties of a proline iminopeptidase from apricot seeds. Keywords Mesh Terms:

KEYWORDS: Substrate Specificity

MESH TERMS: enzymology

Chemical & Substance for Abstract: Purification and properties of a proline iminopeptidase from apricot seeds. Information

Substance Name: prolyl aminopeptidase

Registry Number: EC 3.4.11.5

Grant and Affiliation Information for Purification and properties of a proline iminopeptidase from apricot seeds.

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Country: JAPAN

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MEDLINETA: J Biochem

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