[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.