Association of glyceraldehyde 3-phosphate dehydrogenase with the membrane of the intact human erythrocyte

Abstract

Intact human erythrocytes were exposed to low concentrations of glutaraldehyde. After washing and subsequent lysis of the cells, glyceraldehyde 3-phosphate dehydrogenase activity is associated with a membrane fraction and cannot be eluted by salt treatment. Lactate dehydrogenase activity is associated with a supernatant fraction under the same conditions. Preincubation of the intact cells under conditions designed to increase internal NADH concentrations leads to a lower membrane-associated activity of glyceraldehyde 3-phosphate dehydrogenase after lysis.