Na"',K"-ATPase (EC 3.6.1.3) was purified to homogeneity from the kidney of spontaneously hypertensive rats (SHR), and their normotensive control rats (Wistar Kyoto rats; WKW. Purity of the enzyme was confirmed by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis, in combination with immu noblotting using anti-dog Na+,K*-ATPase antibody. The enzyme purified from SHR and WKY did not differ in respect to the molecular weight, subunit composition, specific activity, ouabain sensitivity, requirements for Na+ and K+ (and also for Mg" and Ca"), and to the extent of heat denaturation. The results indicate that the difference in Na+,K+-pump so far reported between SHR and WKY is not attributable to any difference in biochemical properties of the purified l\la+,K+-ATPase.