The effect of various reductones and their derivatives on glyoxalase enzyme system has been studied with crude enzyme systems extracted from ox or mouse liver, applying the semicarbazide method for the enzyme activity assay. Inhibition spectra of the two enzyme systems were not significantly different from each other. Of polyphenols,
ortho- (catechol, pyrogallol),
meta- (resorcinol, phloroglucinol) and
para- (hydroquinone) dihydroxy derivatives exhibited strong, medium and very weak inhibitory effect respectively. Substitution at 4-position of catechol with polar groups (gallic acid, Dopa) decreased the inhibitory potency of the compounds except for chlorogenic acid.
p-Benzoquinone showed markedly strong inhibition, which might be caused by direct reaction of the compound with one of the substrates, glutathione, to form some new compounds as judged from the results with UV spectrum measurement and paper chromatography. Aliphatic reductones and their related compounds (ascorbic acid, ascorbic acid-3-phosphate, dehydroascorbic acid, triose reductone, diacetyl) exhibited weak or slight inhibitions. Bidentate chelating agents, oxalate and phthalate, showed a little different effects on the two enzyme systems, though the inhibitions were not significantly strong in both cases.
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