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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D003402:Creatine Kinase / Q000302:isolation & purification*; D006736:Horses; D046911:Macromolecular Substances; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D011817:Rabbits; D013045:Species Specificity; D013552:Swine
D000596:Amino Acids; D046911:Macromolecular Substances; D003402:Creatine Kinase