[Hydrophobic properties of various phosphohydrolases].
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.
Uteulin
K R
KR
Dzhakelova
Sh A
ShA
Ivashchenko
A T
AT
Kusainova
N I
NI
D000251:Adenosine Triphosphatases / Q000032:analysis; D000438:Alcohols / Q000494:pharmacology; D000818:Animals; D002384:Catalysis; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004912:Erythrocytes / Q000201:enzymology; D005952:Glucose-6-Phosphatase / Q000032:analysis; D066298:In Vitro Techniques; D008930:Mitochondria, Liver / Q000201:enzymology; D010744:Phosphoric Monoester Hydrolases / Q000032:analysis*; D051381:Rats; D000254:Sodium-Potassium-Exchanging ATPase / Q000032:analysis; D012995:Solubility
D000438:Alcohols; D010744:Phosphoric Monoester Hydrolases; D005952:Glucose-6-Phosphatase; D000251:Adenosine Triphosphatases; D000254:Sodium-Potassium-Exchanging ATPase
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