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.
Subject(s)
Phosphoric Monoester Hydrolases/analysis , Adenosine Triphosphatases/analysis , Alcohols/pharmacology , Animals , Catalysis , Chemical Phenomena , Chemistry, Physical , Erythrocytes/enzymology , Glucose-6-Phosphatase/analysis , In Vitro Techniques , Mitochondria, Liver/enzymology , Rats , Sodium-Potassium-Exchanging ATPase/analysis , SolubilityABSTRACT
The alcohols and anions present at the medium before the beginning of ATPase reaction increased or decreased the lag-time of ATPase hydrolysis by chloroplast coupled factor according to the extent of their inhibitory or stimulating action. The effect of alcohols and anions on the ATPase activity of coupled factor of chloroplasts and mitochondria develops less than 2 s in case of their introduction during the ATP hydrolysis.
Subject(s)
Adenosine Triphosphatases/metabolism , Alcohols/pharmacology , Anions/pharmacology , Chloroplasts/enzymology , Mitochondria, Liver/enzymology , Adenosine Triphosphate/metabolism , Animals , Chloroplasts/drug effects , Enzyme Activation/drug effects , Fabaceae/drug effects , Fabaceae/enzymology , Hydrolysis , Mitochondria, Liver/drug effects , Plants, Medicinal , Rats , Solubility , Time FactorsABSTRACT
The appreciable changes in hydrophobic properties of ATPase of rat liver submitochondrial particles were discovered 3 days after whole-body X-irradiation with a dose of 7 Gy. The sensitivity of ATPase activity to stimulating anions decreased. The radiation damages to ATPase were detected and the ratio of concentrations of magnesium and ATP exceeded a unity.
