Creatine Phosphokinase in Thyroid: Isoenzyme Composition Compared with Other Tissues

Abstract

Considerable creatine phosphokinase activity was demonstrated in thyroid glands of several species. After starch gel electrophoresis, thyroid exhibited a creatine phosphokinase isoenzyme pattern different from that of muscle, heart, and brain. The isoenzyme repertory of various tissues and a hybrid enzyme produced from muscle and brain enzyme are consistent with the postulated dimeric structure of creatine phosphokinase.