Formation of an unusual hybrid in the development of human adenosine 5'-triphosphate-creatine phosphotransferase.

1. Starch-gel analysis of extracts from adult human muscle, heart and brain reveals a hybrid creatine kinase with an abnormally high electrophoretic mobility. 2. Hybridization in vitro confirms that the postulated hybrid is formed from a combination of brain- and muscle-type enzyme sub-units. 3. The relative electrophoretic mobility of the hybrid is not affected by changing the starch concentration in the gel or by the buffer system used, or by electrophoresis in thin layers of Sephadex. 4. It is concluded that hybrid formation results in a net increase on the dimeric enzyme of from 4 to 6 negative charges. 5. During development a sharp increase in the rate of production of muscle-type enzyme sub-units occurs in heart at 10-13 weeks' gestation and in muscle at 18-20 weeks' gestation. The latter change is accompanied by a relative decrease in the concentration of brain-type sub-units.