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Titolo:
PURIFICATION AND CHARACTERIZATION OF THERMOSTABLE DIPEPTIDASE FROM CARP INTESTINE
Autore:
ARANISHI F; WATANABE T; OSATOMI K; CAO MJ; HARA K; ISHIHARA T;
Indirizzi:
NATL RES INST FISHERIES SCI YOKOHAMA KANAGAWA 236 JAPAN NAGASAKI UNIV,FAC FISHERIES,BUNKYO KU NAGASAKI 852 JAPAN NAGASAKI UNIV,GRAD SCH MARINE SCI & ENGN,BUNKYO KU NAGASAKI 852 JAPAN
Titolo Testata:
Journal of marine biotechnology
fascicolo: 2, volume: 6, anno: 1998,
pagine: 116 - 123
SICI:
0941-2905(1998)6:2<116:PACOTD>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
BRUSH-BORDER; PROTEIN DIGESTION; RENAL DIPEPTIDASE; PEPTIDE HYDROLASES; SOLUBLE FRACTIONS; RAT; ABSORPTION; MUCOSA; GLUTATHIONE; ACID;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
40
Recensione:
Indirizzi per estratti:
Citazione:
F. Aranishi et al., "PURIFICATION AND CHARACTERIZATION OF THERMOSTABLE DIPEPTIDASE FROM CARP INTESTINE", Journal of marine biotechnology, 6(2), 1998, pp. 116-123

Abstract

Thermostable dipeptidase was purified to homogeneity from soluble cytoplasmic extract of carp intestine with an increase in specific activity of 372-fold and a 2% recovery rate. The enzyme was determined to have molecular weights of 64,000 after reduction and 320,000 without reduction, indicating that it is composed of five sulfide-linking molecules of subunit peptide chains of identical molar size. The optimum hydrolysis pH and temperature of the enzyme were evaluated by L-leucine-glycine to be pH 9.0 and 60 degrees C, respectively, and it was markedlystable in the alkaline region and at temperatures below 70 degrees C. Dipeptide hydrolysis of the enzyme was inhibited by sulfide-specific and tryptophan-specific inhibitors, reductant and metal chelating reagents. In addition, varying concentrations of EDTA and 1,10-phenanthroline inactivated the enzyme. Sulfide-affinity bivalent metals potently inactivated the enzyme, while Mg2+ and Mn2+ activated it linearly and stepwise, respectively. The enzyme had a narrow range of action on dipeptides of X-glycine and L-leucine-X, but it had marginal or no effecton other dipeptides, tripeptides, and peptide derivatives. Its maximum hydrolysis occurred with L-leucine-L-leucine, and both L-leucine-glycine and L-leucine-L-serine served as preferential substrates.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 00:33:16