Abstract
Summary
The molecular weight and size of myosin from mice with hereditary muscular dystrophy and from their normal litter-mates as controls were studied by various physical-chemical methods. The ultracentri-fugal patterns were similar for the two kinds of myosin, but light scattering seemed to indicate polydispersity of their molecular parameters for dystrophic mice. The ATPase enzymatic activities and the ability to combine with F-actin were not affected by the disease.
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