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Temperature effects on cation affinities of the (Na+, K+)-ATPase of mammalian brain
Authors:Alan C Swann  RWayne Albers
Institution:1. Department of Psychiatry, Yale University School of Medicine, New Haven, CT 06510 U.S.A.;2. Laboratory of Neurochemistry, National Institute of Neurological and Communicative Disorders and Stroke, Bethesda, MD 20857 U.S.A.
Abstract:Effects of temperature on the Na+-dependent ADP-ATP exchange and the p-nitrophenylphosphatase reactions catalysed by (Na+, K+)-ATPase were examined. Apparent Mg2+ affinity decreased with decreasing temperature. Arrhenius plots of p-nitrophenylphosphatase in the presence of Na+ and ATP had discontinuities similar to those previously reported for (Na+ + K+)-ATPase, while those of p-nitrophenylphosphatase measured without Na+ or ATP did not. The apparent activation energy for p-nitrophenylphosphatase was a function of the physical characteristics of the cation acting at the K+ site.
Keywords:Cation regulation  Temperature effect
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