A method is developed for detection and quantitative determination of the creatine kinase isoenzymes during electrophoresis in agar gel. They are found in the agar gel block by formation of fluorescent sites due to combination of the isoenzymes reaction product: creatine with ninhydride in the alkaline medium followed by fluorophore quantitative elution. The method is specific, simple, highly sensitive. It was used to study mobility of creatine kinase of mitochondria and isoenzymes of the rat myocardium mytochondria sarcoplasmic fraction during electrophoresis under different conditions. It is established that mobility of creatine kinase of mitochondria differs from that of isoenzymes. During electrophoresis in agar gel, contrary to polyacrylamide gel, it arranges relative to sarcoplasma isoenzymes depending on the buffer used.

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