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Titolo:
PURIFICATION AND PROPERTIES OF AN AMINOPEPTIDASE FROM A PROTAMINE-DEGRADING MARINE BACTERIUM
Autore:
OBATA H; SUGIYAMA A; KAWAHARA H; MURAMATSU T;
Indirizzi:
KANSAI UNIV,FAC ENGN,DEPT BIOTECHNOL,YAMATECHO 3-3-35 SUITA OSAKA 564JAPAN KANSAI UNIV,HIGH TECHNOL RES CTR SUITA OSAKA 564 JAPAN NAGASAKI UNIV,FAC FISHERIES NAGASAKI 852 JAPAN
Titolo Testata:
Bioscience, biotechnology, and biochemistry
fascicolo: 7, volume: 61, anno: 1997,
pagine: 1102 - 1108
SICI:
0916-8451(1997)61:7<1102:PAPOAA>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEOTIDE-SEQUENCE; ESCHERICHIA-COLI; MONKEY BRAIN; AMINO-ACID; PEPN GENE; ARYLAMIDASE; CLEAVAGE; MUSCLE; ROE;
Keywords:
MARINE BACTERIUM; AMINOPEPTIDASE; AEROMONAS SALMONICIDA; ALANINE AMINOPEPTIDASE; L-ALA-BETA-NAPHTHYLAMIDE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
H. Obata et al., "PURIFICATION AND PROPERTIES OF AN AMINOPEPTIDASE FROM A PROTAMINE-DEGRADING MARINE BACTERIUM", Bioscience, biotechnology, and biochemistry, 61(7), 1997, pp. 1102-1108

Abstract

A protamine-degrading marine bacterium was isolated from marine soil and identified as Aeromonas salmonicida subsq. based on its taxonomical characteristics. An alanine-specific amino-specific aminopeptidase, called aminopeptidase K, from an extract of the strain was purified and characterized. The aminopeptidase K was purified about 80-fold by fractionation with ammonium sulfate and column chromatography on QA-52 cellulose, Phenyl Superose and Superose 12. The purified enzyme is composed of 6 subunits of 86 kDa with a molecular mass of 520 kDa according to gel filtration and SDS-PAGE. The N-terminal sequence of the enzyme was H . -Asp-Tyr-Asp-Ala-Pro-Asp-Tyr-Tyr-Ile-Thr-Ile-Thr-. It is inhibited by monoiodoacetate, N-ethylmaleimide, and puromycin. The Michaelis constant (K-m) and the maximal rate of hydrolysis (V-max) were, respectively, 0.28 mM and 49.4 mu mol/min/mg for the L-Ala-beta-naphthylamide substrate. The optimum pH and optimum pH and optimum temperaturewere 6.5 and 45 degrees C, respectively. The purified enzyme was highly specific to L-Ala-beta-naphthylamide.

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Documento generato il 05/04/20 alle ore 04:01:08