Homodyne measurements of the laser light spectrum scattered from solutions of rabbit skeletal muscle myosin in high ionic-strength media manifested a characteristicD value dependence on myosin concentrations. Using the typicalD versus myosin concentration curves obtained in the presence of 0.5m phosphate and 0.2m 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 measuredD 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.
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Cardinaud, R., Drifford, M. Quasi-elastic light scattering studies of rabbit skeletal myosin solutions. J Muscle Res Cell Motil 3, 313–332 (1982). https://doi.org/10.1007/BF00713040
- Rabbit Skeletal Muscle
- Scattering Study
- Common Argument
- Irreversible Aggregation
- Skeletal Muscle Myosin