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• W1582624231 abstract "Abstract As is well known, the light scattering intensity of F-actin solutions increases immediately upon formation of the rigor complex with subfragment-1 (S-1). We have found that after the initial rise in scattering, there is a further gradual increase in scattering (we call it super-opalescence). Fluorescence and electron microscopic observations of acto-S-1 solutions showed that super-opalescence results from formation of actin filament bundles once S-1 binds to F-actin. The actin bundles possessed transverse stripes with a periodicity of about 350 A, which suggested that in the bundles actin filaments are arranged in parallel register. The rate of the initial process of bundle formation (i.e. side-by-side dimerization) could be approximately estimated by measuring the initial rate of super-opalescence (V0). V0 had a maximum (V0m) at a molar ratio of S-1 to actin of 1;6-1;7, regardless of the actin concentration, pH (6-8.5), Mg2+ concentration (up to 5 mM), or ionic strength (up to 0.3 M KC1). Lower pH, higher Mg2+ concentration, and higher ionic strength increased V0m; V0 was proportional to the square of the actin concentration, regardless of the solution conditions." @default.
• W1582624231 created "2016-06-24" @default.
• W1582624231 creator A5000818695 @default.
• W1582624231 creator A5056997297 @default.
• W1582624231 date "1985-02-01" @default.
• W1582624231 modified "2023-09-30" @default.
• W1582624231 title "Skeletal muscle myosin subfragment-1 induces bundle formation by actin filaments." @default.
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• W1582624231 doi "https://doi.org/10.1016/s0021-9258(18)89557-6" @default.
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