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Titolo:
THE ROLE OF A THIOL PROTEASE IN THE PROTEOLYSIS OF CONNECTIN IN RABBIT SKELETAL-MUSCLE MYOFIBRILS
Autore:
KIMURA S; MAKI S; MARUYAMA K;
Indirizzi:
CHIBA UNIV,FAC SCI,DEPT BIOL CHIBA 263 JAPAN
Titolo Testata:
Biomedical research
, volume: 14, anno: 1993, supplemento:, 2
pagine: 89 - 92
SICI:
0388-6107(1993)14:<89:TROATP>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALPHA-CONNECTIN; ELASTIC PROTEIN; BETA-CONNECTIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
10
Recensione:
Indirizzi per estratti:
Citazione:
S. Kimura et al., "THE ROLE OF A THIOL PROTEASE IN THE PROTEOLYSIS OF CONNECTIN IN RABBIT SKELETAL-MUSCLE MYOFIBRILS", Biomedical research, 14, 1993, pp. 89-92

Abstract

Connectin is easily degraded into beta-connectin and 1,200 kDa fragment when myofibrils prepared from rabbit skeletal muscle were kept at 4-degrees-C. Takahashi et al. (10) claimed that this splitting was due to a direct action of calcium ions, because calcium ions enhanced the degradation in the presence of approximately 0.1 mM leupeptin. However, it turned out that 0.1 mM leupeptin was not enough to prevent the splitting of connectin, but 1 mM leupeptin was required. In the presenceof 1 mM leupeptin, 0.1 mM CaCl2 did not induce connectin breakdown atall. Addition of 0.1% casein completely stopped the connectin splitting, suggesting that the connectin degradation was due to a protease action. 0.1 mM calpastatin, an inhibitor specific to calpain, inhibited proteolysis of connectin. However, since calcium ions were not required for the connectin splitting, it is concluded at the present time that a thiol protease is responsible for connectin splitting in myofibrils.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/07/20 alle ore 05:24:20