Thermal sensitivity of Na+,K+-ATPase isoenzymes in the brain and kidney
Kaplia, A.A.; Kravtsov, A.V.; Kravtsova, V.V.
Ukrainskii Biokhimicheskii Zhurnal 66(6): 58-66
1994
ISSN/ISBN: 0201-8470 PMID: 7785087 Document Number: 434749
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.