Molecular organization of subunits of electroplax (sodium plus potassium)--activated adenosine triphosphatase.
Antisera against each of the two major subunits of detergent-solubilized electroplax (sodium plus potassium)-activated adenosine triphosphatase from Electrophorus electricus were prepared. Antiserum against the small subunit (a glycoprotein, Mr = 58,000) partially inhibits [3H]ouabain binding to the enzyme, but does not interfere with the phosphorylation of enzyme. Conversely, antiserum against the large subunit (the catalytic subunit Mr = 96,000) partially inhibits phosphorylation of the enzyme, but does not interfere with the binding of [3H]ouabain to the enzyme. Since ouabain only interacts with enzyme from the outer surface of the membrane and phosphorylation of enzyme takes place on the inner surface of the membrane, the results suggest that the small subunits are exposed on the outer surface of the membrane, whereas the large subunits are oriented predominantely facing the cytoplasmic side.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D004557:Electric Organ / Q000201:enzymology*; D004593:Electrophorus; D004789:Enzyme Activation; D046911:Macromolecular Substances; D008861:Microsomes / Q000201:enzymology; D008970:Molecular Weight; D011188:Potassium / Q000494:pharmacology; D012964:Sodium / Q000494:pharmacology; D012995:Solubility; D013501:Surface-Active Agents
D046911:Macromolecular Substances; D013501:Surface-Active Agents; D012964:Sodium; D000251:Adenosine Triphosphatases; D011188:Potassium