Abstract
The binding of actin to myosin containing phosphorylated and dephosphorylated light chains (LC 2) was invesfigated by studying the influence of actin on Mg 2+-K + -stimulated ATPase of phosphorylated and dephosphorylated myosin and by comparing the influence of PP i on actomyosin formed from pure actin and phosphorylated or dephosphorylated myosin. The concentration of actin producing inhibition of one half of myosin K + -ATPase activity was 4.1 μM and 7.7 μM for phosphorylated and dephosphorylated myosin, respectively. Actomyosin formed from dephosphorylated myosin dissociated at lower PP i concentration than did that from the phosphorylated form. The extrapolated values for Km obtained from studies of the influence of actin on Mg 2+ -ATPase activity of dephosphorylated myosin were about twice as high as for t phosphorylated form. Thus, the affinity of phosphorylated myosin for actin was significantly higher under all conditions studied.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
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