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- W2039918712 abstract "The interaction of dehydroretronecine, a hepatocarcinogenic metabolite of the pyrrolizidine alkaloid monocrotaline, with yeast alcohol dehydrogenase (ADH), cysteine and bovine serum albumin (BSA) was studied. Dehydroretronecine inhibited ADH with an inhibition constant (Ki) of 3.38 × 10−2 m at pH 7.5 and 25 °C. No inhibitory effect was observed when excess cysteine was added to the assay system. The interaction of dehydroretronecine with cysteine was demonstrated by spectrophotometric titration. Titration of dehydroretronecine alone at 240 nm showed an apparent pK value of 5.0. whereas titration of dehydroretronecine in the presence of excess cysteine resulted in an increase of pK from 5.0 to 8.5. Equilibrium dialysis data indicated appreciable binding of dehydroretronecine to BSA at pH 4.2 and 6°C." @default.
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- W2039918712 date "1977-01-01" @default.
- W2039918712 modified "2023-09-26" @default.
- W2039918712 title "Inhibition of yeast alcohol dehydrogenase by dehydroretronecine" @default.
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- W2039918712 doi "https://doi.org/10.1016/s0015-6264(77)80006-0" @default.
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