Histochemical Demonstration of Sodium–Potassium-activated Adenosinetriphosphatase in Normal and Leukaemic Granulocytes

Abstract

SODIUM–POTASSIUM-activated adenosinetriphosphatase (Na–K-ATPase) is an enzyme regulating the active cation transport through the cell wall¹. This enzyme differs from other ATPases in its great sensitivity to cardiac glycosides, and is inhibited by ouabain (strophantine G) at a 10⁻⁵ M concentration². Na–K-ATPase systems have been demonstrated in various animal and human tissues^1,3,4. In 1964 Block and Bonting⁵ found Na–K-ATPase activity in leucocyte suspensions isolated from human blood. The close relation of this enzyme to the active transport of sodium and potassium in granulocytes was demonstrated. Block and Bonting also observed a significant increase in ATPase activity in leucocyte suspensions taken from cases of acute and chronic myelocytic leukaemia and chronic lymphocytic leukaemia⁵.