Quasi-elastic Light Scattering Studies of Rabbit Skeletal Myosin Solutions

Overview

Journal J Muscle Res Cell Motil

Specialties Cell Biology
Physiology

Date 1982 Sep 1

PMID 7130378

Citations 2

Authors

R CARDINAUD

M Drifford

Affiliations

Soon will be listed here.

Abstract

Homodyne measurements of the laser light spectrum scattered from solutions of rabbit skeletal muscle myosin in high ionic-strength media manifested a characteristic D value dependence on myosin concentrations. Using the typical D versus myosin concentration curves obtained in the presence of 0.5 M phosphate and 0.2 M phosphate respectively as references, it has been shown that: (1) the observed phenomena are completely reversible; (2) minor components such as C- and F-protein do not significantly influence the measured D values; and (3) the effect of preparation procedures on these dynamic light-scattering measurements is negligible. A common argument (irreversible aggregation) against a monomer-dimer equilibrium is ruled out; on the other hand, some doubt still remains with regard to the existence and physiological significance of a reversible dimerization.

Citing Articles

Electric birefringence study of rabbit skeletal myosin subfragments HMM, LMM, and rod in solution.

CARDINAUD R, Bernengo J Biophys J. 1985; 48(5):751-63.

PMID: 4074835 PMC: 1329400. DOI: 10.1016/S0006-3495(85)83833-9.

A simple and rapid preparation of fully phosphorylated and fully dephosphorylated skeletal muscle myosin. Application to the preparation of a phosphorylated LC2-modified artificial isozyme.

CARDINAUD R J Muscle Res Cell Motil. 1986; 7(5):455-66.

PMID: 3025253 DOI: 10.1007/BF01753588.

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