Native myosin from adult rabbit skeletal muscle: isoenzymes and states of aggregation

Biochemistry
J E MorelF Piot

Abstract

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).

References

Sep 20, 1986·Journal of Molecular Biology·N BachouchiJ E Morel
Nov 22, 1982·FEBS Letters·J E Morel, M Garrigos
Sep 1, 1982·Journal of Muscle Research and Cell Motility·R Cardinaud, M Drifford
Feb 1, 1993·Journal of Muscle Research and Cell Motility·S S MargossianH S Slayter
Mar 27, 1997·Biophysical Chemistry·K ClaireS Highsmith

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Citations

Apr 1, 2000·Biochimica Et Biophysica Acta·J M Morel, N D'Hahan
Nov 24, 1999·Biochimica Et Biophysica Acta·J MorelG Figuera Picazo
Jul 18, 2006·Journal of Theoretical Biology·Enrico Grazi, Cristina Di Bona

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