This study was undertaken to localize the enzyme sodium-potassium dependent adenosine triphosphatase in unstimulated human small lymphocytes using the histochemical technique of McClurkin [1964]. The substrate adenosine 5' triphosphate is hydrolyzed by the ATPase resulting in a lead phosphate precipitate at the site of enzyme action, subsequently visualized as lead sulphide.The enzyme was demonstrated in three different patterns, and for each donor the pattern was constant both on all four of the test slides, and on different occasions. The patterns observed were: clusters of granules related to the cell membrane; positive staining localized to portions of the cell membrane, and, less commonly, the whole cell circumference. The significance of this distribution may relate to areas with large numbers of antigen recognition sites on the lymphocyte membrane.Coulson [1969] suggested that the antigen recognition site on sensitized small lymphocytes was a unique three dimensional structure incorporated in the cell membrane, that micro-deformation of the membrane occurred following sterochemical recognition of a specific antigen at the site, and that the resulting membrane distortion was transduced by non-specific cholinesterase and ATPase [Duncan, 1967] to initiate an intracellular stimulation pathway. Since the hypothesis was first proposed, cholinesterase has been demonstrated on small lymphocyte cell membranes [Coulson, 1970], and more recently Ellegaard and Dimitrov [1973] have demonstrated the existence of two different ATPase activities in homogenates of human lymphocytes, one of which was ouabain sensitive and possibly associated with the cell membranes. These findings are consistent with the probable existence of at least two ATPases in the cell, one associated with mitochondria and oxidative phosphorylation, and another associated with cation transport [Roodyn, 1967].The study described in this paper was undertaken with small lymphocytes prior to any stimulation as part of an evaluation of the enzyme systems in the small lymphocyte which would be available in the event of antigenic stimulation. In particular, a search was undertaken for any unusual arrangement of the membrane ATPase in view of its postulated role as an antigen recognition site marker. By using the cytochemical technique developed by McClurkin [1964] it was hoped not only to confirm the existence of ATPase in the small lymphocyte membrane but also to investigate its distribution, in keeping with Lison's 181