Separation of Two Different Heavy Meromyosins

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Abstract
Heavy meromyosin prepared from rabbit skeletal myosin by chymotryptic digestion was separated into two different heavy meromyosins by Sepharose 4B-6 aminohexyl PP1 column chromatography. SDS-gel electrophoresis of one fraction of heavy meromyosin, which was eluted with 75 mM ammonium acetate, showed that it contained the small polypeptide chains, g3 and g2 as well as the large chains. The other fraction of heavy meromyosin, which was eluted with 85 mM ammonium acetate, contained g1 and g2 We concluded that the two heavy meromyosins arose from two different populations (isozymes) of myosin. No significant difference in Ca2+-ATPase activity was detected between the two heavy meromyosins.