Abstract
SOME of the properties of the enzyme creatine phosphokinase have recently been described1; but no experiments were reported on the activity of the enzyme with substrates other than adenosine tri-phosphate, adenosine diphosphate, phosphocreatine and creatine. Such experiments are in progress and will be reported in due course. A recent publication by Armstrong2, in which it was shown that the administration of N-ethylglycocyamine (negmine) was followed by the urinary excretion of N-ethyl-glycocyamidine (negmidine), suggested that a phosphorylation reaction may have been involved. It was therefore of interest to determine whether negmine could be phosphorylated by the creatine phosphokinase system.
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References
Ennor, A. H., and Rosenberg, H., Biochem. J., 57, 203 (1954).
Armstrong, M. D., Fed. Proc., 12, 170 (1953).
Ennor, A. H., and Rosenberg, H. (unpublished observations).
Lipmann, F., “Adv. in Enzymol.”, 1, 99 (1941).
Borsook, H., and Dubnoff, J. W., J. Biol. Chem., 168, 493 (1947).
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ENNOR, A., ROSENBERG, H. & ARMSTRONG, M. Specificity of Creatine Phosphokinase. Nature 175, 120 (1955). https://doi.org/10.1038/175120a0
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DOI: https://doi.org/10.1038/175120a0


