• Publications
  • Influence
The (Na+ + K+)-activated ATPase. Enzymatic and transport properties.
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Substrate sites for the (Na+ + K+)-dependent ATPase.
  • J. D. Robinson
  • Chemistry, Medicine
  • Biochimica et biophysica acta
  • 13 May 1976
Kinetic studies on a rat brain (Na+ + K+)-dependent ATPase (EC 3.6.1.3) preparation demonstrated high-affinity sites for ATP, with a Km near 1 mum, and low affinity sites for ATP, with a Km near 0.5Expand
  • 117
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Uptake and release of calcium by rat brain synaptosomes
Rat brain synaptosomes, prepared by discontinuous Ficoll density gradient centrifugation, accumulated 45Ca during brief incubations in modified Krebs-Ringer media. Uptake of 45Ca was increased by 5Expand
  • 101
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Rapid kinetic analyses of the Na+/K(+)-ATPase distinguish among different criteria for conformational change.
The Na+/K(+)-ATPase couples the hydrolysis of ATP to the transport of Na+ and K+ via a phosphorylated intermediate and conformational changes. In order to identify these conformational changes, weExpand
  • 38
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SPECIFIC MODIFICATIONS OF THE Na+, K+‐DEPENDENT ADENOSINE TRIPHOSPHATASE BY DIMETHYL SULFOXIDE *
  • J. D. Robinson
  • Biology, Medicine
  • Annals of the New York Academy of Sciences
  • 1 January 1975
DMSO inhibits the Na+, K+-ATPase, but stimulates the associated K+-phosphatase activity. For the ATPase, DMSO acts as an uncompetitive inhibitor toward both ATP and Na+, whereas it increases the K0.5Expand
  • 21
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Kinetics of conformational changes associated with potassium binding to and release from Na+/K(+)-ATPase.
The Na+/K(+)-ATPase functions in cells to couple energy from the hydrolysis of ATP to the transport Na+ out and K+ in. The fluorescent probe IAF (iodoacetamidofluorescein) covalently binds to thisExpand
  • 7
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Cerebroside sulfate (sulfatide A) in some organs of the rat and in a mast cell tumor.
A noteworthy characteristic of cerebroside sulfate (2) (sulfatide A (3)) is its continual accumulation in the brain of rats (4), human beings (5), and mice (6). Recent experiments (7) withExpand
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Interactions between monovalent cations and the (Na+ + K+)-dependent adenosine triphosphatase.
  • J. D. Robinson
  • Chemistry, Medicine
  • Archives of biochemistry and biophysics
  • 1 July 1970
Abstract Kinetic properties of a (Na + + K + )-dependent ATPase preparation from rat brain were examined as functions of the concentrations of activating monovalent cations, in terms of: K 0.5 , theExpand
  • 84
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Functionally distinct classes of K+ sites on the (Na+ + K+)-dependent ATPase.
  • J. D. Robinson
  • Chemistry, Medicine
  • Biochimica et biophysica acta
  • 28 March 1975
K+ interactions with a rat brain (Na+ + K+)-dependent ATPase and the associated K+-dependent nitrophenyl phosphatase activity were examined. Classes of sites for K+ were distinguished, initially, onExpand
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