[A comparative study of the intracellular regulation of transport ATPase activity in non-nucleated erythrocytes].

Removing the basic cytoskeleton proteins (spectrin, 4.1 and 2.1 band proteins) from the unnuclear erythrocyte membranes of four mammalian species (mouse, hamster, guinea, pig and rabbit) made no changes in Na,K-ATPases, while the specific activity of Ca-ATPases was decreased (the decreasing was of a range of 60-90% depending on the species, in values per mg of protein). The specific activity of the Na,K-ATPase (per ml of cells) varied from 20 to 30% in different species. Incubation of ghosts with erythrocyte haemolysates from rat led to a markedly expressed activation of the Na,K-ATPase in in erythrocytes of all species studied, while the incubation with erythrocyte haemolysate of the same species caused activation of the enzyme in mouse and guinea pig ghosts only. The data obtained support a concept of intracellular Na,K-ATPase activator (probably a protein) having no absolute species specificity. They also show that normal transport function of ATPases in unnuclear erythrocytes needs integrity of the membrane skeleton.