Beta-ethoxyacrolein contamination increases malondialdehyde inhibition of milk xanthine oxidase activity.
beta-Ethoxyacrolein (BEA), a side product that forms during the preparation of malondialdehyde (MDA) by acidic hydrolysis of tetraethoxypropane (TEP), has been found to be an inhibitor of milk xanthine oxidase (XO) several times more potent than pure MDA (NaMDA). The incubation of XO with 10 microM BEA abolished 50% of the enzyme activity within 1 min; the inhibited enzyme was totally regenerated by dialysis and filtration through Sephadex. The BEA inhibition mode of the enzyme was mixed-type with the apparent inhibition constants (Ki) of 2.4 x 10(-6) M. An HPLC method for quantitation of BEA in the crude commonly used MDA preparation was set up.
Cighetti
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Department of Medical Chemistry and Biochemistry, Faculty of Medicine, University of Milan, Italy. skinski@imiucca.csi.unimi.it
Debiasi
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Ciuffreda
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Allevi
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D000171:Acrolein / Q000031:analogs & derivatives* / Q000494:pharmacology; D000818:Animals; D004340:Drug Contamination; D004347:Drug Interactions; D007700:Kinetics; D008315:Malondialdehyde / Q000494:pharmacology*; D008892:Milk / Q000201:enzymology*; D012996:Solutions; D014969:Xanthine Oxidase / Q000037:antagonists & inhibitors*
D012996:Solutions; C022940:beta-ethoxyacrolein; D008315:Malondialdehyde; D000171:Acrolein; D014969:Xanthine Oxidase