ATP synthesis by the (Na + + K +)-ATPase in the absence of an ionic gradient Effects of organic solvent

A 200-fold decrease in the P i concentration required for half-maximal phosphorylation of the (Na + + K +)-ATPase is observed when 40% (v/v) dimethyl sulfoxide is added to the assay medium. The phosphoenzyme formed in the presence of dimethyl sufoxide is able to transfer its phosphate to ADP to form...

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Bibliographic Details
Published in:FEBS letters 1987-09, Vol.222 (1), p.163-166
Main Authors: de Moraes, Vera Lucia Goncalves, de Meis, Leopoldo
Format: Article
Language:English
Subjects:
(Na + + K +)-ATPase
Adenosine Triphosphate - biosynthesis
Analytical, structural and metabolic biochemistry
Animals
ATP synthesis
Biological and medical sciences
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hydrolases
Kidney - enzymology
Kinetics
Organic solvent effect
Phosphates - metabolism
Phosphorylation
Sheep
Sodium-Potassium-Exchanging ATPase - metabolism
Solvents
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Summary:A 200-fold decrease in the P i concentration required for half-maximal phosphorylation of the (Na + + K +)-ATPase is observed when 40% (v/v) dimethyl sulfoxide is added to the assay medium. The phosphoenzyme formed in the presence of dimethyl sufoxide is able to transfer its phosphate to ADP to form ATP when 400 mM NaCl is added to the medium. The synthesis of ATP depends on the concentrations of organic solvent and of Na +, and is inhibited by ouabain.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(87)80212-0