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  • Title: Crystallization and properties of creatine kinase from equine skeletal muscle.
    Author: Takasawa T, Fukushi K, Shiokawa H.
    Journal: J Biochem; 1981 May; 89(5):1619-31. PubMed ID: 7275956.
    Abstract:
    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.
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