beta-Ethoxyacrolein (BEA), a side product that forms during the prepar
ation of malondialdehyde (MDA) by acidic hydrolysis of tetraethoxpropa
ne (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 mu M BEA abolished 50% of the enzyme activity within 1 min
; the inhibited enzyme was totally regenerated by dialysis and filtrat
ion through Sephadex. The BEA inhibition mode of the enzyme was mixed-
type with the apparent inhibition constants (K-i) of 2.3 x 10(-6) M. A
n HPLC method for quantitation of BEA in the crude commonly used MDA p
reparation was set up. (C) 1998 Elsevier Science Inc.