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Ukr Biokhim Zh (1978) ; 68(2): 51-7, 1996.
Article in Russian | MEDLINE | ID: mdl-9005662

ABSTRACT

Electrophoretic properties of the protein bands of Na+, K(+)-ATPase catalytic subunits of the kidney and brain have been comparatively studied for some types of animals after heat treatment of the preparations in the presence of DS-Na. The diffuse protein zone with lower electrophoretic mobility after heat-induced conformational transformation of alpha appears on gels parallel with protein band alpha II which is typical of this process. The prolonged heat treatment causes more rapid electrophoretic degradation of the alpha-isoform of the Na+, K(+)-ATPase catalytic subunit of the brain in comparison with alpha +. The results of the investigations are discussed in the aspect of existence of heat-induced transformation of the protein-detergent complexes of catalytic subunits of the enzyme.


Subject(s)
Brain/enzymology , Isoenzymes/analysis , Kidney/enzymology , Sodium-Potassium-Exchanging ATPase/analysis , Animals , Catalysis/drug effects , Cattle , Detergents , Electrophoresis, Polyacrylamide Gel/methods , Female , Hot Temperature , Indicators and Reagents , Isoenzymes/drug effects , Isoenzymes/metabolism , Male , Rats , Sodium Dodecyl Sulfate , Sodium-Potassium-Exchanging ATPase/drug effects , Sodium-Potassium-Exchanging ATPase/metabolism , Swine
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