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Pig kidney Na+,K+-ATPase. Primary structure and spatial organization
Authors:Modyanov" target="_blank">N N Ovchinnikov YuAModyanov  N E Broude  K E Petrukhin  A V Grishin  N M Arzamazova  N A Aldanova  G S Monastyrskaya  E D Sverdlov
Abstract:cDNAs complementary to pig kidney mRNAs coding for alpha- and beta-subunits of Na+,K+-ATPase were cloned and sequenced. Selective tryptic hydrolysis of the alpha-subunit within the membrane-bound enzyme and tryptic hydrolysis of the immobilized isolated beta-subunit were also performed. The mature alpha- and beta-subunits contain 1016 and 302 amino acid residues, respectively. Structural data on the peptides from extramembrane regions of the alpha-subunit and on glycopeptides of the beta-subunit underlie a model for the transmembrane arrangement of Na+,K+-ATPase polypeptide chains.
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