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Abstract
Oxalate and glycolate were synthesized from 14C-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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Article info
Publication history
Accepted:
May 12,
1971
Received:
February 10,
1971
Footnotes
☆This work was supported in part by Grant AM-09406 from the United States Public Health Service.
Identification
Copyright
© 1971 Published by Elsevier Inc.