Abstract
Monoatomic alcohols at definite concentration stimulated or inhibited activities of liver mitochondrial ATPase, anion-sensitive ATPase in erythrocyte membranes and Na, K-ATPase in rat brain depending on the ratio of concentrations of the natural substrate components--Mg2+ complex and ATP. Interrelationships between the enzymes and alcohols hydrophobic properties were found.
MeSH terms
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Adenosine Triphosphatases / analysis
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Alcohols / pharmacology
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Animals
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Catalysis
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Chemical Phenomena
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Chemistry, Physical
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Erythrocytes / enzymology
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Glucose-6-Phosphatase / analysis
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In Vitro Techniques
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Mitochondria, Liver / enzymology
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Phosphoric Monoester Hydrolases / analysis*
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Rats
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Sodium-Potassium-Exchanging ATPase / analysis
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Solubility
Substances
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Alcohols
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Phosphoric Monoester Hydrolases
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Glucose-6-Phosphatase
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Adenosine Triphosphatases
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Sodium-Potassium-Exchanging ATPase