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Titolo:
PURIFICATION AND CHARACTERIZATION OF AN EXTRACELLULAR METALLOPROTEASEFROM PSEUDOMONAS-FLUORESCENS
Autore:
KIM HJ; TAMANOUE Y; JEOHN GH; IWAMATSU A; YOKOTA A; KIM YT; TAKAHASHI T; TAKAHASHI K;
Indirizzi:
TOKYO UNIV PHARM & LIFE SCI,SCH LIFE SCI,LAB MOL BIOCHEM,1432-1 HORINOUCHI HACHIOJI TOKYO 19203 JAPAN TOKYO UNIV PHARM & LIFE SCI,SCH LIFE SCI,LAB MOL BIOCHEM HACHIOJI TOKYO 19203 JAPAN UNIV TOKYO,GRAD SCH SCI,DEPT BIOPHYS & BIOCHEM,BUNKYO KU TOKYO 113 JAPAN KIRIN BREWERY CO LTD,CENT LABS KEY TECHNOL YOKOHAMA KANAGAWA 236 JAPAN UNIV TOKYO,INST MOL & CELL BIOSCI,BUNKYO KU TOKYO 113 JAPAN
Titolo Testata:
Journal of Biochemistry
fascicolo: 1, volume: 121, anno: 1997,
pagine: 82 - 88
SICI:
0021-924X(1997)121:1<82:PACOAE>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
PSEUDOMONAS-AERUGINOSA; ERWINIA-CHRYSANTHEMI; ALKALINE PROTEASE; ACID; PROTEINASE; SECRETION; MEMBRANES; SEQUENCE; FAMILIES; CLONING;
Keywords:
CO2+ ION ACTIVATION; METALLOPROTEASE; PARTIAL AMINO ACID SEQUENCE; PSEUDOMONAS FLUORESCENS; SEQUENCE HOMOLOGY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
24
Recensione:
Indirizzi per estratti:
Citazione:
H.J. Kim et al., "PURIFICATION AND CHARACTERIZATION OF AN EXTRACELLULAR METALLOPROTEASEFROM PSEUDOMONAS-FLUORESCENS", Journal of Biochemistry, 121(1), 1997, pp. 82-88

Abstract

An extracellular metalloprotease was purified from the culture supernatant of Pseudomonas fluorescens strain KT1 to apparent homogeneity and shown to consist of a single polypeptide chain (M(r) 46,000-17,000). The enzyme was strongly inhibited by chelating agents such as EDTA and o-phenanthroline, and activated by certain detergents. Among the peptidyl 4-methylcoumaryl-7-amide (MCA) substrates examined, t-butyloxycarbonyl-Arg-Val-Arg-Arg-MCA was the best one, With this substrate, the enzyme exhibited a pH optimum of around pH 5.5 in the absence of Co2+ ions, whereas it showed two different pH optima (at plls around 5.5 and 8-9) in the presence of Co2+ ions due to remarkable activation by Co2+ ions in the alkaline pH range, On the other hand, a single broad pHoptimum of around 6 to 8 was obtained with some peptides in both the presence and absence of Co2+ ions, and no activation by Co2+ was observed, The enzyme showed trypsin-like specificity, preferentially cleaving certain arginyl peptide bonds, and hydrolyzed the basic protein, histone, most rapidly among various proteins examined, Partial amino acid sequence analysis revealed that the enzyme is highly homologous withproteases of the serralysin family, a group of zinc metalloproteases.

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Documento generato il 26/01/21 alle ore 04:43:32