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Titolo:
ISOLATION AND CHARACTERIZATION OF UREA-RESISTANT STAPHYLOCOCCUS-AUREUS V8 PROTEASE DERIVATIVES
Autore:
YABUTA M; ONAIMIURA S; OHSUYE K;
Indirizzi:
SUNTORY INST MED RES & DEV,2716-1 KURAKAKE TOKYO GUNMA 37005 JAPAN
Titolo Testata:
Journal of fermentation and bioengineering
fascicolo: 3, volume: 80, anno: 1995,
pagine: 237 - 243
SICI:
0922-338X(1995)80:3<237:IACOUS>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI; PURIFICATION; SEQUENCE;
Keywords:
RANDOM MUTAGENESIS; UREA RESISTANCE; STAPHYLOCOCCUS AUREUS V8 PROTEASE; EXPRESSION IN ESCHERICHIA COLI;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
19
Recensione:
Indirizzi per estratti:
Citazione:
M. Yabuta et al., "ISOLATION AND CHARACTERIZATION OF UREA-RESISTANT STAPHYLOCOCCUS-AUREUS V8 PROTEASE DERIVATIVES", Journal of fermentation and bioengineering, 80(3), 1995, pp. 237-243

Abstract

Three different urea-resistant Staphylococcus aureus Y8 protease derivatives (V8 Delta 53-U1, V8 Delta 53-U5 and V8 Delta 53-U8) were obtained by random mutagenesis using a polymerase chain reaction (PCR) method. From DNA sequence analysis of the mutants, three different amino acid substitutions, D44E, N71S and K147R, were identified. The half-lives of these mutant enzymes were 3 to 5 times longer than that of the wild type in the presence of 5 M urea, and they also showed increased stability to sodium dodecyl sulfate. Measurements of the kinetic parameter values of each mutant enzyme indicate that these mutations substantially conferred the stability to these denaturants without markedly changing their kinetic parameter values. In addition, we demonstrate that these mutant enzymes were applicable to digestion of a human calcitonin fusion protein produced in Escherichia coli.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 01:23:37