[Structural organization of Na+,K+-ATPase isoenzymes in the plasma membrane].
A current state of the researches related to structural arrangement of the Na+,K(+)-ATPase in the plasma membrane determining high lipid dependence of the enzyme has been reviewed. The membrane properties of the Na+,K(+)-ATPase isozymes, which specific features have been ascertained when investigating their thermal stabilities, sensitivities to phospholipases, detergents, etc., are considered more in detail. The existence of differences in structural organization of boundary lipids of the neuronal Na+,K(+)-ATPase catalytic subunit isoforms is supposed. The adaptive significance of the revealed specificity of the neuronal lipid microenvironment of the Na+,K(+)-ATPase isoforms is assumed.
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O.V. Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv.
D002462:Cell Membrane / Q000201:enzymology; D007527:Isoenzymes / Q000737:chemistry*; D008563:Membrane Lipids / Q000737:chemistry; D010446:Peptide Fragments / Q000737:chemistry*; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry*; D013329:Structure-Activity Relationship
D007527:Isoenzymes; D008563:Membrane Lipids; D010446:Peptide Fragments; D000254:Sodium-Potassium-Exchanging ATPase
Strukturnaia organizatsiia izofermentov Na+,K+-ATPazy v plasmaticheskoĭ membrane.