Isolation and Characterization of Human Skeletal Muscle Creatine Kinase |
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Authors: | William A. Warren |
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Affiliation: | The Mary Imogene Bassett Hospital , Cooperstown, New York, 13326 |
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Abstract: | Human skeletal muscle creatine kinase was purified by isoelectric focusing with a yield of greater than 60%. Two enzymic proteins, differing in specific activity, were obtained, and each final product produced only a single protein band when examined by electrophoretic methods. The proteins were composed of two subunits of about 41, 000 daltons each, and the amino acid compositions were similar. |
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