Reaction of glycolaldehyde with proteins: latent crosslinking potential of alpha-hydroxyaldehydes.

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Abstract
The Schiff base adducts of glyceraldehyde with Hb undergo Amadori rearrangement to form stable ketoamine structures; this reaction is similar to the nonenzymic glucosylation of proteins. The analogous rearrangement of the Schiff base adducts of glycolaldehyde with proteins was demonstrated. However, the Amadori rearrangement of this Schiff base adduct produces a new aldehyde function, an aldoamine, which is generated in situ and is capable of forming Schiff base linkages with another amino group, leading to covalent crosslinking of proteins. Sodium dodecyl sulfate gel electrophoresis of the glycoladehyde-RNase A adduct showed the presence of dimers, trimers and tetramers of RNase A, demonstrating the crosslinking potential of this .alpha.-hydroxyaldehyde. The crosslinked products exhibited an absorption band with a maximum around 325 nm and fluoresence around 400 nm when excited at 325 nm. The crosslinking reaction, the formation of a 325-nm absorption band and the development of fluorescence were prevented when the the incubation was carried out in the presence of sodium cyanoborohydride. The Amadori rearrangement that generates a new carbonyl function is a crucial step in this covalent crosslinking. Glycolaldehyde could be a bifunctional reagent of unique utility because its crosslinking potential is latent, expressed only on completion of the primary reaction.