Species variability of erythrocyte transport ATPases in mammals.

Na+, K(+)-ATPase, and Ca(2+)-ATPase in whole erythrocytes from five species of mammals (rat, mouse, guinea pig, golden hamster, rabbit) after cell treatment with Tween 20 (7.5 mg/ml) varied over a wide range: from 3.0 +/- 0.9 mumol Pi/hr/ml cells in rabbit to 27.3 +/- 4.9 mumol Pi/hr/ml cells in mouse for Na+, K(+)-ATPase and from 8.0 +/- 1.6 mumol Pi/hr/ml cells in hamster to 47.2 +/- 4.9 mumol Pi/hr/ml cells in mouse for Ca(2+)-ATPase. Differences were less pronounced in red cell ghosts. Fatty acid and phospholipid compositions of erythrocyte membranes were similar for all species. Nevertheless, the activity of Ca(2+)-ATPase in ghosts significantly correlated (r = -0.884) with the ratio of PC + SM/PE + PS in red cell membranes. Rabbit membranes had the lowest content of arachidonate. Rat hemolysate activated Na+, K(+)-ATPase in the ghosts from the animals of any species investigated, whereas the enzyme activation by the homohemolysate was characteristic only of the rat, mouse, and guinea pig ghosts. The data obtained suggest that there are differences in both activity and intracellular control of transport ATPase in erythrocytes of different mammals.