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• W2103709097 abstract "The properties of stable acetaldehyde-protein adducts, using bovine serum albumin as a model protein, were investigated. Upon prolonged incubation at 37°C and pH 7.4, the reaction of acetaldehyde and albumin yielded stable adducts that exhibited fluorescent properties. Reaction mixtures of acetaldehyde with polylysine or ethylamine also formed fluorescent products with similar fluorescent spectral properties like acetaldehyde-albumin adducts, indicating that the amino groups of protein alone can generate fluorescent products on reaction with acetaldehyde. When reactions of acetaldehyde with albumin or polylysine were conducted at 22°C, stable binding reached a maximum after 24 hr of incubation and essentially remained at this level during the remaining 216 hr of incubation, and minimal-to-no fluorescence was associated with this binding. At 37°C, stable binding was greater and increased continuously over the entire 216 hr of incubation. After an initial lag period of 24 to 48 hr, increases in fluorescence intensity paralleled the increases in stable binding. The presence of sodium cyanoborohydride, which reduces Schiff bases, in the reaction mixtures prevented fluorescence, indicating that Schiff bases are intermediates in the formation of fluorescent products. Both stable binding and fluorescence intensities were minimally affected by exhaustive dialysis (up to 144 hr), indicating that the fluorescent products were quite stable. These results suggest that an initial reaction of a Schiff base with another acetaldehyde molecule via an aldol condensation reaction gives rise to the formation of a crotonaldehyde Schiff base derivative. This reactive intermediate could then undergo further condensation reactions and form advanced conjugated products, some of which could be fluorescent." @default.
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• W2103709097 date "1993-02-01" @default.
• W2103709097 modified "2023-10-18" @default.
• W2103709097 title "Reaction of Acetaldehyde with Proteins: Formation of Stable Fluorescent Adducts" @default.
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• W2103709097 doi "https://doi.org/10.1111/j.1530-0277.1993.tb00728.x" @default.
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