PMID: 77Nov 20, 1975

Kinetic studies and effects of anions on creatine phosphokinase from skeletal muscle of rhesus monkey (Macaca mulatta)

Biochimica Et Biophysica Acta
W R Chegwidden, D C Watts


A purification procedure for creatine kinase (EC from muscle of the monke35--170 muequiv H+/mg protein per min at 30 degrees C and a yield of approx. 0.5 g/kg muscle. Assuming equilibrium kinetics, synergistic binding of substrates at one catalytic site is found for both the forward and back reactions. Kinetic constants for the binding of each substrate to the free enzyme and the enzyme-second substrate complex are determined and are compared with those for the enzyme from other species. Inhibition by small anions is determined in the presence of different combinations of substrates and products. SO4(2-) inhibits by simple competitive inhibition and probably binds at the site of the transferrable phosphoryl group. Inhibition by NO3-, NO2-, SCN- and Cl- is more complex and these ions are suggested to mimic the transferrable phosphoryl group in a planar transition-state complex. These anions stabilize the dead-end complex, enzyme-creatine-MgADP, which lacks the transferable phosphoryl group. The effects of these anions on the dissociation constants of the enzyme-substrate complexes is reported and is in accord with the above hypothesis. The dead-end complex in the absence of anion does not protect the essential thiol gro...Continue Reading


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