[Thermolability of alpha+-isoform of the catalytic subunit of brain Na+,K+-ATPase].
Thermal stabilities of Na+,K(+)-ATPase isozymes from the rat brain and kidney tissues are compared. It is established that heat treatment of Na+,K(+)-ATPase preparations from the brain decreases the high affinity component of the ouabain inhibition of the enzyme activity due to selective inactivation of alpha-isoform. Its higher thermal lability in comparison with alpha-isoform is confirmed.
Kaplia
A A
AA
Kravtsov
A V
AV
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002384:Catalysis; D004795:Enzyme Stability; D005260:Female; D006358:Hot Temperature; D007527:Isoenzymes / Q000037:antagonists & inhibitors* / Q000378:metabolism; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D046911:Macromolecular Substances; D008297:Male; D010042:Ouabain / Q000494:pharmacology; D010766:Phosphorylation; D051381:Rats; D000254:Sodium-Potassium-Exchanging ATPase / Q000037:antagonists & inhibitors* / Q000378:metabolism
D007527:Isoenzymes; D046911:Macromolecular Substances; D010042:Ouabain; D000254:Sodium-Potassium-Exchanging ATPase
Termolabil'nost' alpha+-izoformy kataliticheskoĭ sub''edinitsy Na+,K+-ATP-azy mozga.