Das Verhalten von Triphospho-pyridinnucleotid, Flavinadenin-dinucleotid, Coenzym A und Thiaminpyrophosphat in Hämolysaten von Kaninchen-Reticulocyten und -Erythrocyten

Abstract

The lowering of the rate of glycolysis on hemolyzing erythrocytes was traced to increased breakdown of adeno-sine triphosphate (ATP) and diphosphopyridine nucleotide (DPN). He-molysis also damages glycolysis in reticulocytes, but here fortification of the hemolysate with ATP and DPN did not lead to a restoration of glycolysis. The fate in hemolysates of other coenzymes was therefore investigated in order to locate blocks in reaction sequences. It was found that FAD and CoA were stable, while TPN and TPP were decomposed slowly. This rate of decomposition was too small to account for the decreased rate of glycolysis following hemolysis. It was found that the content of ATP and FAD of reticulocytes was about twice as high as that of erythrocytes. It was also shown that hemolysates catalyze the synthesis of TPN from niacin and ATP.