Dog myocardial myosin preparations, purified according to the procedures presented here, utilizing either one or two (NH4)2SO4fractionations, contained no major contaminants which could be detected by disc gel electrophoresis, and exhibited high myosin ATPase activity. The low molecular weight components (light chains) were dissociated from the rest of the molecule by denaturing with urea; the chains were further purified by column chromatography. Procedures were a modification of those used for purification of skeletal muscle myosin light chains. According to immunoanalyses the two myocardial myosin light chains showed antigenic specificity.
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