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Article Dans Une Revue Biochemistry Année : 1998

Native Myosin from Adult Rabbit Skeletal Muscle: Isoenzymes and States of Aggregation

Nathalie d'Hahan
  • Fonction : Auteur
Karima Taouil
  • Fonction : Auteur
Mathilde Francin
Asuncion Aguilar
  • Fonction : Auteur
Jean-Pierre Dalbiez
  • Fonction : Auteur
Zalika Merah
  • Fonction : Auteur
Hélène Grussaute
  • Fonction : Auteur
Benoît Hilbert
  • Fonction : Auteur
Frédérique Ollagnon
  • Fonction : Auteur
Gersendre Selva
  • Fonction : Auteur
François Piot
  • Fonction : Auteur

Résumé

The globular heads of skeletal muscle myosin have been shown to exist as isoenzymes S1 (A1) and S1 (A2), and there are also isoforms of the heavy chains. Using capillary electrophoresis, we found two dominant isoenzymes of the whole native myosin molecule, in agreement with what has previously been found by various techniques for native and nondenatured myosin from adult rabbits. Findings about possible states of aggregation of myosin and its heads are contradictory. By analytical ultracentrifugation, we confirmed the existence of a tail-tail dimer. By laser light scattering, we found a head-head dimer in the presence of MgATP. Capillary electrophoresis coupled with analytical ultracentrifugation and laser light scattering led us to refine these results. We found tail-tail dimers in a conventional buffer. We found tail-tail and head-head dimers in the presence of 0.5 mM MgATP and pure head-head dimers in the presence of 6 mM MgATP. All the dimers were homodimers. Naming the dominant isoenzymes of myosin a and b, we observed tail-tail dimers with isoenzyme a (TaTa) and with isoenzyme b (TbTb) and also head-head dimers with isoenzyme a (HaHa) and with isoenzyme b (HbHb).

Dates et versions

hal-03299779 , version 1 (26-07-2021)

Identifiants

Citer

Jean-Emile Morel, Nathalie d'Hahan, Karima Taouil, Mathilde Francin, Asuncion Aguilar, et al.. Native Myosin from Adult Rabbit Skeletal Muscle: Isoenzymes and States of Aggregation. Biochemistry, 1998, 37 (16), pp.5457-5463. ⟨10.1021/bi972384k⟩. ⟨hal-03299779⟩

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