Abstract
An enzyme fraction which specifically catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate has been isolated and partially purified from goat liver. The enzyme fraction appears to be substantially free from glyoxalase I, reduced glutathione, and triosephosphate isomerase. Approximately equimolar quantities of methylglyoxal and inorganic phosphate were obtained from dihydroxyacetone phosphate. Formation of methylglyoxal was confirmed by colorimetric and enzymatic estimations as well as by paper chromatography and its spectrum. Glyceraldehyde-3-phosphate, fructose 1,6-bisphosphate, dihydroxyacetone, and glyceraldehyde, failed to act as substrates. The enzyme is inhibited by some phosphorylated compounds and inorganic phosphates.
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