title: [Isolation of Na+, K+-ATP-ase].
abstract: The data are discussed on the isolation of Na+, K+-ATPase from the membrane structures of a cell at functionally active state. The isolation of the membrane enzymes, particularly multicomponent enzymic systems, which might include Na+, K+-ATPase, is a rather complex task as their components are ordered in the membrane in a certain way. The disturbance of this ordering that is essentially maintained by membrane phospholipids, results in the inactivation of the enzymatic system. Different procedures are compared permitting the Na+, K+ATPase isolation and purification to be realized. It is noted that when realizing the Na+, K+-ATPase isolation and purification by means of a number of non-ionic detergents it is possible to obtain the "soluble" Na+, K+-ATPase preparations from the membrane structures, the preparations being a convenient initial material for the further purification of this enzymic system and its obtaining as a "functionally intact unit". The Na+, K+-ATPase isolation as a "functionally intact unit" would probably make an essential contribution to deciphering the molecular mechanism of the Na+ and K+ transport through biomembranes.
mesh_terms: D000251:Adenosine Triphosphatases / Q000302:isolation & purification*; D000818:Animals; D001665:Binding Sites; D001693:Biological Transport, Active; D001921:Brain / Q000201:enzymology; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D007672:Kidney Cortex / Q000201:enzymology; D008566:Membranes / Q000201:enzymology; D008722:Methods; D008861:Microsomes / Q000201:enzymology; D011188:Potassium / Q000378:metabolism; D051381:Rats; D012964:Sodium / Q000378:metabolism; D012995:Solubility; D013363:Submandibular Gland / Q000201:enzymology; D013501:Surface-Active Agents; D013552:Swine
chemical_list: D013501:Surface-Active Agents; D012964:Sodium; D000251:Adenosine Triphosphatases; D011188:Potassium
vernacular_title: Vydelenie Na+,K+-ATF-azy