Inhibition of oxalate synthesis: in vitro studies using analogues of oxalate and glycolate.

摘要: Abstract Fourteen analogues of oxalate or glycolate were studied as potential inhibitors synthesis. Their inhibitory properties determined in human erythrocytic preparations, which the enzymatic activity seems to be predominantly, if not exclusively, lactic dehydrogenase (LDH), and a partially purified glycolic acid oxidase preparation from rat liver. Evidence is presented that, liver, nicotinamide-adenine dinucleotide (NAD)-dependent oxidation, probably catalyzed by LDH, major pathway for synthesis rather than flavin mononucleotide (FMN)-dependent oxidation oxidation. Of analogues, oxalatehydrazide was found most potent inhibitor LDH-catalyzed None very active an oxidase. Hydroxymethanesulfonate demonstrated effective compound inhibition. Five its structural analogues-acetoxymethanesulfonate, aminomethanesulfonate, iodomethanesulfonate, chloromethanesulfonate, fluoromethanesulfonate—were less two vitro systems used. Other approaches control are discussed. These studies furnish background testing vivo .