Water-soluble Subfraction in Myosin A Preparation***

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Abstract
Rabbit muscle myosin A was fractionated by ammonium sulfate or subjected to DEAE-cellulose column chromatography at pH 7.4. Untreated, chromatographed, and ammonium sulfate-fractionated myosin A preparations demonstrated the elution patterns from DEAE-cellulose column, slightly differing from each other. Release of 0.45 saturated ammonium sulfate[long dash]sol. subtractions during incubation of untreated or ammonium sulfate-fractionated myosin a preparations in 0.25M KCl-0.1 M phosphate buffer (pH 7.0) at 35 [degree]C proceeded with time, whereas DEAE-cellulose treated myosin A gave only a slight release of the soluble protein. Those three myosin A preparations showed approximately equal ATPase activity, while DEAE-cellulose[long dash]treated myosin A exhibited a slightly higher actin- binding than untreated myosin A. The released protein is most likely an impurity not related to myosin A itself.