Inactivation of brain Na+,K(+)-ATPase catalytic subunit isoforms by sodium dodecyl sulfate.
Persistence of the brain and kidney Na+,K(+)-ATPase isozymes to SDS inactivation under different time and temperature conditions of microsome extraction with the detergent was compared. In contrast to enzyme preparations from medulla oblongata the higher sensitivity of the Na+,K(+)-ATPase alpha-isoform (in comparison to alpha +) to SDS inactivation accompanied by its, at least, partial removal from the membrane was found in the preparations from cerebral cortex. This difference in the sensitivity to SDS was eliminated after extraction of microsomes with the detergent at 37 degrees C. The interpretation of the results is based on the assumed differences in the structural organization of the boundary lipids of the neuronal Na+,K(+)-ATPase catalytic subunit isoforms.
Kaplya
A
A
Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kiev, Ukraine.
Kravtsova
V V
VV
Kravtsov
A V
AV
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002417:Cattle; D003902:Detergents / Q000494:pharmacology*; D004791:Enzyme Inhibitors / Q000494:pharmacology; D007527:Isoenzymes; D007668:Kidney / Q000201:enzymology; D008861:Microsomes / Q000201:enzymology; D010042:Ouabain / Q000494:pharmacology; D051381:Rats; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology*; D000254:Sodium-Potassium-Exchanging ATPase / Q000037:antagonists & inhibitors*
D003902:Detergents; D004791:Enzyme Inhibitors; D007527:Isoenzymes; D012967:Sodium Dodecyl Sulfate; D010042:Ouabain; D000254:Sodium-Potassium-Exchanging ATPase