Crystallization and properties of creatine kinase from equine skeletal muscle.
A crystalline creatine kinase was obtained from equine skeletal muscle. The enzyme was homogeneous, as judged by ultracentrifugation and disc electrophoresis on polyacrylamide gel. The crystalline enzyme had a specific activity of 110 units per mg of protein, that is, 14-fold purification over the crude extract of equine skeletal muscle. The molecular weight of the enzyme was determined to be 84,600 by the conventional low-speed sedimentation equilibrium method, and s020,w was 5.32S. Eight cysteine residues were found on amino acid analysis, two of which were essential for the enzymatic activity.
D000577:Amides / Q000032:analysis; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002499:Centrifugation, Density Gradient; D003402:Creatine Kinase / Q000302:isolation & purification*; D003460:Crystallization; D006736:Horses / Q000378:metabolism*; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D013438:Sulfhydryl Compounds / Q000032:analysis; D014364:Tryptophan / Q000032:analysis
D000577:Amides; D000596:Amino Acids; D013438:Sulfhydryl Compounds; D014364:Tryptophan; D003402:Creatine Kinase