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This paper reports inhibition of Na(+) + K(+)-stimulated, ouabain-inhibited adenosine triphosphatase (S-ATPase) in sheep red cell membranes by oxidized glutathione (GSSG). The results are consistent with the hypothesis that this inhibition depends upon the formation of a mixed disulfide between glutathione and -SH group(s) in the enzyme protein. Thus, inhibition of S-ATPase by GSSG proceeds more rapidly at alkaline than at neutral pH and is reversed by the addition of an excess of a compound containing reduced -SH groups (e.g. dithiothreitol). ATP protects S-ATPase against inhibition by GSSG and this protection depends on both the monovalent and divalent cation composition of the medium. Protection by ATP is more complete in the presence of K(+) than in the presence of Na(+).

Inhibition of Adenosine Triphosphatase in Sheep Red Cell Membranes by Oxidized Glutathione