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. 1966 Sep;100(3):762–767. doi: 10.1042/bj1000762

Temperature-dependence of activation and inhibition of rat-brain adenosine triphosphatase activated by sodium and potassium ions

N Gruener 1, Y Avi-Dor 1
PMCID: PMC1265212  PMID: 16742417

Abstract

1. The adenosine-triphosphatase activity of rat-brain microsomes was measured between 0° and 37°. The stimulatory effect of Na+ plus K+ on the Mg2+-dependent adenosine-triphosphatase activity decreased sharply with decreasing temperature and became negligible at 0°. An Arrhenius plot drawn from the experimental data showed two discontinuities: one at about 6° and the other at about 20°. 2. The increment in activity induced by Na+ plus K+ was more sensitive to oligomycin at lower than at higher temperatures, but the opposite was observed for ouabain. The action of oligomycin showed a biphasic character, since below a certain concentration it caused slight activation of Na+-plus-K+-activated adenosine triphosphatase. 3. Where oligomycin increased the activity of the enzyme, it also enhanced the accumulation of an acid-precipitable phosphorylated compound formed through the transfer of the γ-phosphate group of [32P]ATP to the enzyme system. Stimulatory concentrations of oligomycin did not interfere with K+-mediated dephosphorylation of the intermediate, though high concentrations of oligomycin counteracted the effect of K+. 4. The temperature profile of K+-stimulated microsomal phosphatase qualitatively resembled that of microsomal adenosine triphosphatase.

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Selected References

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