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. 1975 Jan;244(3):731-9.
doi: 10.1113/jphysiol.1975.sp010822.

The interaction of ATP-analogues possessing a blocked gamma-phosphate group with the sodium pump in human red cells

T J Simons

The interaction of ATP-analogues possessing a blocked gamma-phosphate group with the sodium pump in human red cells

T J Simons. J Physiol. 1975 Jan.

Abstract

1. The (Na++K+)-ATPase of red cell membranes is unable to hydrolyse ATP-analogues in which the oxygen atom linking the beta- and gamma-phosphate groups is replaced by a minusCH2minus or minusNH-bridge. 2. In resealed ghosts both these ATP-analogues support K:K exchange but not Na:K exchange. ATP supports both modes of operation of the sodium pump, whereas neither occurs without any nucleotide. 3. These results support the hypothesis that ATP is needed as a cofactor for K:K exchange to occur, and make it extremely unlikely that phosphorylation from ATP is involved.

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