Subcellular fractions were isolated from homogenates of human and rat gastric mucosal membranes by means of differential centrifugation; the highest Na+, K(+)-ATPase activity was detected in microsomal fraction. The enzymatic activity was higher in human gastric mucosal membrane as compared with the rat tissue. Na+, K(+)-ATPase activity was inhibited by 0.1% SDS added into the homogenization mixture. Ouabain 1.5 x 10(-3) M did not affect the enzymatic activity. The enzyme had a pH optimum in both these tissues at pH 7.2 = 7.4 in 30 mM imidazol-HCl buffer and at pH 7.1-7.2 in 40 mM Tris-HCl buffer. K+ exhibited maximal activating effect at 20 mM concentration in human gastric mucosal membrane and at 5 mM concentration in rat tissue. The ratio ATP/Mg2+ as 1:1 proved to be optimal at 2 mM concentration.
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