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Titolo:
ACTIVATION OF THE 20S PROTEASOME OF XENOPUS OOCYTES BY CARDIOLIPIN - BLOCKAGE OF THE ACTIVATION OF TRYPSIN-LIKE ACTIVITY BY THE SUBSTRATE
Autore:
YAMADA S; SATO K; URITANI M; TOKUMOTO T; ISHIKAWA K;
Indirizzi:
UNIV SHIZUOKA,FAC SCI,DEPT BIOL & GEOSCI,836 OYA SHIZUOKA 4228529 JAPAN UNIV SHIZUOKA,FAC SCI,DEPT CHEM SHIZUOKA 4228529 JAPAN
Titolo Testata:
Bioscience, biotechnology, and biochemistry
fascicolo: 6, volume: 62, anno: 1998,
pagine: 1264 - 1266
SICI:
0916-8451(1998)62:6<1264:AOT2PO>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
MULTICATALYTIC PROTEINASE COMPLEX; SODIUM DODECYL-SULFATE; RAT-LIVER; REVERSIBLE ACTIVATION;
Keywords:
20S PROTEASOME; TRYPSIN-LIKE ACTIVITY; ACTIVATOR CARDIOLIPIN; XENOPUS OOCYTES; CONFORMATIONAL CHANGE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
13
Recensione:
Indirizzi per estratti:
Citazione:
S. Yamada et al., "ACTIVATION OF THE 20S PROTEASOME OF XENOPUS OOCYTES BY CARDIOLIPIN - BLOCKAGE OF THE ACTIVATION OF TRYPSIN-LIKE ACTIVITY BY THE SUBSTRATE", Bioscience, biotechnology, and biochemistry, 62(6), 1998, pp. 1264-1266

Abstract

The effects of an activator, cardiolipin, on the three peptidase activities of the 20S proteasome of Xenopus oocytes were examined. The trypsin-like activity was activated when the enzyme was treated with cardiolipin before the addition of the substrate, but there was no appreciable activation when cardiolipin was added concomitantly with the substrate. On the other hand, the chymotrypsin-like peptidase and peptidylglutamylpeptide hydrolase (PGPH) were activated regardless of the sequence of addition. When very low concentrations of the substrate (e.g. 0.1-0.5 mu M; about 1/100 of the K-m) were used, cardiolipin strongly activated trypsin-like peptidase by the simultaneous addition but not after substrate addition. These results suggest that the trypsin-type substrate produces a conformational change in the enzyme in a concentration-dependent manner which makes the activator sites inaccessible tocardiolipin.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 21:34:26