TY - JOUR
T1 - Ouabain binding to sodium and potassium dependent adenosine triphosphatase
T2 - inhibition by the β,γ methylene analogue of adenosine triphosphate
AU - Tobin, T.
AU - Akera, T.
AU - Hogg, R. E.
AU - Brody, T. M.
PY - 1973
Y1 - 1973
N2 - To determine the mechanism of nucleotide dependent, Na+ stimulated binding of [3H]ouabain to (Na+ + K+)-ATPase (EC 3.6.1.3.), we tested the ability of β, γ methylene ATP (adenylylmethylenediphosphonate) to support [3H]ouabain binding. β, γ Methylene ATP is an analogue of AN ANALOGUE OF ATP in which the β and γ phosphates are linked by a methylene group. It is not hydrolyzed by the (Na+ + K+)-ATPase. In the presence of Na+ and Mg++, β, γ methylene ATP did not support [3H]ouabain binding to rat brain (Na+ + K+)-ATPase and it inhibited ATP dependent binding. When [3H]ouabain binding to guinea pig kidney (Na+ + K+)-ATPase was determined in the presence of Na+, Mg++, and Pi, the addition of β, γ methylene ATP was inhibitory, in contrast to the stimulation produced by ATP. The results show that β, γ methylene ATP binds to the (Na+ + K+)-ATPase and that this interaction does not support [3H]ouabain binding.
AB - To determine the mechanism of nucleotide dependent, Na+ stimulated binding of [3H]ouabain to (Na+ + K+)-ATPase (EC 3.6.1.3.), we tested the ability of β, γ methylene ATP (adenylylmethylenediphosphonate) to support [3H]ouabain binding. β, γ Methylene ATP is an analogue of AN ANALOGUE OF ATP in which the β and γ phosphates are linked by a methylene group. It is not hydrolyzed by the (Na+ + K+)-ATPase. In the presence of Na+ and Mg++, β, γ methylene ATP did not support [3H]ouabain binding to rat brain (Na+ + K+)-ATPase and it inhibited ATP dependent binding. When [3H]ouabain binding to guinea pig kidney (Na+ + K+)-ATPase was determined in the presence of Na+, Mg++, and Pi, the addition of β, γ methylene ATP was inhibitory, in contrast to the stimulation produced by ATP. The results show that β, γ methylene ATP binds to the (Na+ + K+)-ATPase and that this interaction does not support [3H]ouabain binding.
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M3 - Article
C2 - 4268124
AN - SCOPUS:0015863859
SN - 0026-895X
VL - 9
SP - 278
EP - 281
JO - Molecular Pharmacology
JF - Molecular Pharmacology
IS - 2
ER -