Isolation and properties of creatine kinase from porcine skeletal muscle

Creatine kinase has been isolated in a good yield from porcine skeletal muscle. The enzyme was purified about 8-fold from crude extract of porcine skeletal muscle in a yield of about 44%. The purified enzyme was homogeneous, as judged by sedimentation velocity (S020,W=5.31S), sedimentation equilibrium, and polyacrylamide gel electrophoresis. The molecular weight of the enzyme was determined to be 83,200 by high-speed meniscus-depletion sedimentation equilibrium analysis. The molecular weight of its subunit was estimated to be 43,000-44,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The amino acid composition of the enzyme was determined.