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The interaction of ATP‐analogues possessing a blocked gamma‐phosphate group with the sodium pump in human red cells.
Author(s) -
Simons T J
Publication year - 1975
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1113/jphysiol.1975.sp010822
Subject(s) - sodium pump , atp hydrolysis , sodium , phosphate , nucleotide , phosphorylation , adenosine triphosphate , chemistry , cofactor , atpase , membrane , biochemistry , biophysics , atp synthase , intracellular , enzyme , biology , organic chemistry , ouabain , gene
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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