Intact human erythrocytes were exposed to low concentrations of glutaraldehyde. After washing and subsequent lysis of the cells, glyceraldehyde 3-phosphate dehydrogenase activity is found to be 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.

No abstract

The binding site for glyceraldehyde 3-phosphate dehydrogenase on the membrane of the intact erythrocyte is not yet known, although studies on lysed erythrocytes would suggest a specific association of the enzyme with the 'Band 111' glycoprotein component of the plasma membrane (Yu & Steck, 1975;