Association of glyceraldehyde 3-phosphate dehydrogenase with the membrane of the intact human erythrocyte.
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.
D004910:Erythrocyte Membrane / Q000201:enzymology*; D004912:Erythrocytes / Q000201:enzymology; D005976:Glutaral / Q000494:pharmacology; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000097:blood*; D006801:Humans; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000097:blood; D009243:NAD / Q000097:blood; D010084:Oxidation-Reduction
D009243:NAD; D007770:L-Lactate Dehydrogenase; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D005976:Glutaral