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- W2072393504 abstract "The present work investigates the effect of malondialdehyde (MDA) binding on the enzymic activity and on some structural properties of glucose 6-phosphate dehydrogenase (G6PD). We studied whether alpha-crystallin could protect the enzyme against MDA damage, and if so, by what mechanism. We also studied whether alpha-crystallin could renature G6PD denatured by MDA. alpha-Crystallin was prepared from bovine lenses by gel chromatography. MDA was freshly prepared and incubated with G6PD with or without alpha-crystallin. The results show that MDA reacted with G6PD non-enzymically causing inactivation at concentrations lower than those used previously on structural proteins. The modified enzyme became fluorescent. alpha-Crystallin, acting as a molecular chaperone, specifically protected the enzyme against inactivation by MDA. The enzyme was not reactivated by alpha-crystallin, but it was stabilised and protected against further denaturation. Complex formation between alpha-crystallin and the modified enzyme was demonstrated by immunoprecipitation. G6PD was very susceptible to MDA and we have shown for the first time that alpha-crystallin is able to protect the enzyme against this damage." @default.
- W2072393504 created "2016-06-24" @default.
- W2072393504 creator A5079028463 @default.
- W2072393504 creator A5089752643 @default.
- W2072393504 date "2000-01-01" @default.
- W2072393504 modified "2023-10-17" @default.
- W2072393504 title "α-Crystallin protects glucose 6-phosphate dehydrogenase against inactivation by malondialdehyde" @default.
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- W2072393504 doi "https://doi.org/10.1016/s0925-4439(99)00087-3" @default.
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