INACTIVATION OF GREATINE KINASE AT LOW UREA CONCENTRATIONS IS NOT DUE TO THE DISSOCIATION OF THE DIMERIC ENZYME
肌酸激酶在低浓度脲溶液中失活也非二聚体解聚所致

Dissociation of dimeric creatine kinases in urea solutions of different concentrations was studied by hybridization of the muscle and brain enzymes (MM and BB) from rabbit It has been found that the enzyme has been mostly inactivated in low urea concentrations, it is still in the dimeric state or only very little was dissociated. It appears therefor that in low urea concentrations, inactivation of creatine kinase is not due to the dissociation of the active dimer. The present result supports that the conformational state of the active site of this enzyme is very fragile and easily disrupted.