Purification and Characterization of a 43,000 Dalton “DNAase Binding Protein” Distinct from Acti1

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Abstract
“DNase binding protein” of 43K daltons as determined by SDS-polyacrylamide gel electrophoresis, was purified from the 0.1 M KCI-soluble (non-structural) fraction of chicken skeletal muscle. The protein was distinct from actin in amino acid composition and physicochemical properties. “DNase binding protein” was also isolated from other kinds of muscle and non-muscle cells. The ratio of the amino acid incorporation rate of “DNAase binding protein” to that of actin is different between skeletal and smooth muscle and non-muscle cells.