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  • Title: Isolation of creatine kinase BB isoenzyme with high specific activity and adequate purity for radioimmunoassay from human placenta on preparative polyacrylamide gel electrophoresis.
    Author: Geng JG, Cheng HZ, Yang YF, Qian ZH, Jiang CY.
    Journal: Clin Chim Acta; 1989 Apr 28; 181(1):1-10. PubMed ID: 2498018.
    Abstract:
    This report describes the procedures for isolation of creatine kinase BB isoenzyme (CK-BB) from human placenta on preparative polyacrylamide gel electrophoresis. 2.5 mg of CK-BB was purified from a 100-g portion of the human placenta, which had a mean specific activity of 957 kU/g and a mean yield of 16%. The placenta CK-BB exhibited single protein bands on several electrophoretic techniques. In addition, both of the placenta and brain CK-BB preparations were individually iodinated and the identical immunological properties of both the CK-BB preparations were confirmed in radioimmunoassay.
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