[Thermal sensitivity of Na+,K+-ATPase isoenzymes in the brain and kidney].
Thermal stabilities of Na+, K(+)-ATP-ase preparations with different isozyme content from brain and kidneys of different animal species have been compared. The greater thermal lability of the alpha(+)-isoform of a catalytic subunit of Na+, K(+)-ATP-ase is established. The method of specific thermal inactivation of in brain preparations was used in comparative study of ouabain sensitivity of Na+, K(+)-ATP-ase isozymes from rat, cow and rabbit. It is concluded that the existing structural and functional model of the receptor site of Na+, K(+)-ATP-ase catalytic subunit is not sufficient for the complete explanation of the species heterogeneity of Na+, K(+)-ATP-ase affinity to heart glycosides.
Kaplia
A A
AA
Kravtsov
A V
AV
Kravtsova
V V
VV
D000818:Animals; D001665:Binding Sites; D001921:Brain / Q000201:enzymology*; D002384:Catalysis; D002417:Cattle; D004795:Enzyme Stability; D006358:Hot Temperature; D007668:Kidney / Q000201:enzymology*; D011817:Rabbits; D051381:Rats; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry*; D013329:Structure-Activity Relationship
D000254:Sodium-Potassium-Exchanging ATPase
Termochuvstvitel'nost' izofermentov Na+,K+-azy mozga i pochek.