Abstract
About one mole of DTNB-light chain per mol of myosin was removed from rabbit myosin by heat-treatment at 30°C for 10min in a solution containing 2mM EDTA, 30mM KCl, and 20mM Tris-HCl (pH 8.5). The above treated myosin (RabM(-LC)) could bind rabbit myosin DTNB-light chain or regulatory light chains of several molluscan myosins. However, the affinity of RabM(-LC) to molluscan regulatory light chains was estimated to be approx. 1/7 times lower than that to DTNB-light chain. The binding of molluscan regulatory light chain to RabM(-LC) practically did not affected both actomyosin Mg-ATPase activity and superprecipitation activity of acto-RabM(-LC), thus conferring no Ca2+-sensitivity.
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