Purification and characterization of an aminopeptidase from porcine liver.

Purification and characterization of an aminopeptidase from porcine liver. Research Abstract Details 

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Purification and characterization of an aminopeptidase from porcine liver. Abstract Text:

S Kawata,T Imamura,K Ninomiya,S Makisumi,

An aminopeptidase was purified about 700-fold from porcine liver homogenate by ammonium sulfate fractionation and a series of column chromatographies on DEAE-cellulose, Sephadex G-150, DEAE-Sepharose, and hydroxyapatite. The purified enzyme had a specific activity of 4.6 mumol X min-1 X mg-1 using L-leucine beta-naphthylamide as the substrate. The molecular weight of the enzyme was about 96,000 as determined by Sephadex G-150 column chromatography. The enzyme had a broad specificity and a pH optimum between 6.5 and 7.0 for hydrolysis of alpha-aminoacyl-beta-naphthylamines, and it hydrolyzed the beta-naphthylamides of aliphatic, basic, and aromatic amino acids. The enzyme also hydrolyzed peptide substrates with phenylalanine residues as their amino-termini, but it did not hydrolyze L-phenylalanyl-L-proline. The enzyme was inhibited by metal-chelating agents, sulfhydryl reagents, heavy metals, bestatin, and puromycin. Activity of the enzyme inhibited by sulfhydryl-reactive reagents was restored by the addition of sulfhydryl compounds. The enzyme was activated by cobaltous ion and the values of both Km and Vmax increased. The activation was pH-dependent and above pH 7.5 cobalt ion behaved as an inhibitor of the enzyme. No metal ions other than cobaltous ion stimulated the enzyme appreciably.

Purification and characterization of an aminopeptidase from porcine liver. Publishing Authors By Initials

S Kawata,T Imamura,K Ninomiya,S Makisumi,

For similar animals: chordata: vertebrates: mammals: artiodactyla: swine research abstracts see: animals: chordata: vertebrates: mammals: artiodactyla: swine research

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Purification and characterization of an aminopeptidase from porcine liver. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 92

Page Numbers: 1093-101

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Oct

YEAR: 1982

Purification and characterization of an aminopeptidase from porcine liver. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Purification and characterization of an aminopeptidase from porcine liver. Keywords Mesh Terms:

KEYWORDS: Swine

MESH TERMS: enzymology

Chemical & Substance for Abstract: Purification and characterization of an aminopeptidase from porcine liver. Information

Substance Name: Amino Acid Naphthylamidases

Registry Number: EC 3.4.11.-

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Country: JAPAN

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MEDLINETA: J Biochem

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