Presence of the Glycolytic Enzymes D-Glyceraldehyde-3-Phosphate Dehydrogenase Phosphoglycerate Kinase and Triosephosphate Isomerase in Hemolysates of Preserved Blood

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Abstract
The presence of glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate kinase and triosephosphate isomerase was shown in hemolysates prepared from human red cells preserved 5-22 days in an acid citrate-dextrose solution at 5[degree]. In order t o demonstrate these enzymes with fructose diphosphate as substrate it is necessary to supplement the endogenous hemolysate aldolase with the rabbit muscle enzyme. Under appropriate conditions it is also possible to demonstrate the oxidation of reduced diphosphopyridine nucleotide (DPNH2) by a reversal of the phosphoglycerate kinase and glyceraldehyde-3-phosphate dehydrogenase reactions, beginning with 3-phosphoglycerate, adenosine triphosphate and DPNH2 as substrates. The significance of the findings relative to the failure of glycolysis in preserved blood is discussed.