Suppression of creatine kinase-catalyzed phosphotransfer results in increased phosphoryl transfer by adenylate kinase in intact skeletal muscle.

@article{Dzeja1996SuppressionOC,
  title={Suppression of creatine kinase-catalyzed phosphotransfer results in increased phosphoryl transfer by adenylate kinase in intact skeletal muscle.},
  author={Petras P. Dzeja and Robert J. Zeleznikar and Nelson D. Goldberg},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 22},
  pages={12847-51}
}
The kinetics of creatine kinase (CK) and adenylate kinase (AK) activities were monitored in intact diaphragm muscle by 18O phosphoryl oxygen exchange to assess whether these two phosphotransferases provide an interrelated function integral to high energy phosphoryl metabolism. This possibility was examined by quantitating the net rates of CK- and AK-catalyzed phosphoryl transfer in comparison to the total cellular ATP metabolic rate when CK activity in the intact diaphragm muscle was… CONTINUE READING