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Titolo:
CALPONIN INHIBITS ACTIN-ACTIVATED MGATPASE OF MYOSIN SUBFRAGMENT-1 (S1) WITHOUT DISPLACING S1 FROM ITS BINDING-SITE ON ACTIN
Autore:
KOLAKOWSKI J; KARKUCINSKA A; DABROWSKA R;
Indirizzi:
M NENCKI INST EXPT BIOL,DEPT MUSCLE BIOCHEM,3 PASTEUR ST PL-02093 WARSAW POLAND M NENCKI INST EXPT BIOL,DEPT MUSCLE BIOCHEM PL-02093 WARSAW POLAND
Titolo Testata:
European journal of biochemistry
fascicolo: 3, volume: 243, anno: 1997,
pagine: 624 - 629
SICI:
0014-2956(1997)243:3<624:CIAMOM>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
SMOOTH-MUSCLE CALPONIN; F-ACTIN; ACTOMYOSIN MGATPASE; ATPASE ACTIVITY; CALDESMON; MECHANISM; PROTEINS;
Keywords:
CALPONIN; MYOSIN SUBFRAGMENT 1; ACTIN-BINDING; ACTOMYOSIN ADENOSINE-TRIPHOSPHATASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
42
Recensione:
Indirizzi per estratti:
Citazione:
J. Kolakowski et al., "CALPONIN INHIBITS ACTIN-ACTIVATED MGATPASE OF MYOSIN SUBFRAGMENT-1 (S1) WITHOUT DISPLACING S1 FROM ITS BINDING-SITE ON ACTIN", European journal of biochemistry, 243(3), 1997, pp. 624-629

Abstract

Calponin is a smooth-muscle thin-filament protein implicated in the regulation of contraction. Its binding to actin is a prerequisite for inhibition of actin-activated myosin MgATPase. Investigating the molecular mechanism of this inhibition, it was found that titration of acto-myosin subfragment 1 with calponin in the presence of either ADP or ATP does not displace weakly or strongly bound myosin subfragment 1 (S1)from actin. S1 . ADP, however, is able to release about two-thirds ofthe calponin from saturated (equimolar) complexes of actin-calponin. The remaining calponin is sufficient for almost full inhibition of acto-S1 MgATPase activity. Bundling of actin filaments by calponin takes place at a higher ratio calponin/actin (above 1:3) and, therefore, is not responsible for inhibition of the ATPase. Bundle formation is inhibited by S1 . ADP. These results suggest the existence of two calponin-binding sites on actin; one, that is insensitive to S1, which is responsible for inhibition of the ATPase, the other, from which calponin is readily displaced by S1.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 10:15:14