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KMID : 0385219920020020121
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Korean Journal of Gerontology
1992 Volume.2 No. 2 p.121 ~ p.132
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Studies on the Methylglyoxal Reductase as a Possible Glycation Inhibitor
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Yang Ryung
Jang Moon-Sang
Shin Dong-Bum
Oh Doo-Hwan
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Abstract
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Methylglyoxal reductase from porcine liver was purified and its biochemical properties were studied. The molecular weight of the enzyme was estimated to be 36,000 dalton and 39,000 dalton by gel filtration and SDS-PAGE, respectively. These results suggested that methylglyxal reductase acts as monomeric enzyme in situ. Methylglyoxal reductase in this study had higher NADH-dependent activity than NADPH-dependent activity. The optimum pH was pH 6.5∼7.0 and the enzyme was more highly sensitive to sulfhydryl group reagents. The enzyme had high activites toward 2-oxoaldehyde such as methylglyoxal and considered to be involved in the control of glycation (Maillard reaction) in the body.
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KEYWORD
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methylglyoxal, methylglyoxal reductase, maillard reaction, polymerization, self-defense enzyme
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