Abstract
Abstract Oxalate and glycolate were synthesized from 14 C-glyoxylate by leukocytes, erythrocytes, and dialyzed hemolysate preparations. Oxalate decarboxylase was used in a convenient and reliable assay of oxalate produced. Leukocytes were approximately 10 to 20 times as active in oxalate and glycolate synthesis, respectively, as erythrocytes. Data submitted to indicate that the erythrocytic enzyme system is lactic dehydrogenase (LDH) include nicotinamide, adenine dinucleotide dependence, pH curve, simultaneous glycolate and oxalate synthesis, inhibition by oxalate and oxamate, and coincidence of isoenzyme activities for lactate and glyoxylate. Coincidence of glyoxylate and lactate oxidation by LDH isoenzymes was also shown in leukocyte preparations. These findings are discussed in terms of the implications of the coupling by LDH of glyoxylate oxidation to oxalate and its reduction to glycolate or the competitive reduction of another substrate. The implications for the development of a pharmacologic inhibitor of oxalate synthesis are also presented.
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