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The maximum amount of acid-stable phosphoenzyme (E32P)/mol of alpha chain of pig gastric H/K-ATPase from [gamma-32P]ATP (K(1/2) = 0.5 microM) was found to be approximately 0.5, which was half of that(More)
The modification of Na+,K+-ATPase with increasing pyridoxal 5'-diphospho-5'-adenosine (AP2PL) concentrations resulted in saturation of the approximately 0.5 mol AP2PL probe incorporation into the(More)
To investigate the relationship between the high and the low affinity ATP-binding site, which appears during the Na(+)/K(+)-ATPase reaction, four amino acids were mutated, the side chains of which(More)