Sites of Protein Glycation

Starting with a synthetic heptapeptide, /V M.ys-Lys-/j-Ala-Lys-/3-Ala-Lys-Gly, and equimolecular amounts of glucose or lactose (2 h, 110 °C, pH 6.7), the sites and nature of glycation were determined using MALDI-TOF-MS, collision-induced 

Capillary electrophoresis is a powerful separation technique. Hinton and Ames162 subjected BSA (1 mM) to capillary electrophoresis, incubating it alone or with gly-oxal (25 mM) in phosphate buffer (pH 7.5) at 37 °C for 14 d. Electropherograms of the 5 kDa fractions from tryptic digests exhibited 70 peaks with some unique to each sample. 

Chevalier el al,163 glycated /j-lactoglobulin (0.217 mM) with equimolar amounts of ribose, arabinose, galactose, glucose, rhamnose, or lactose at 60 °C in 0.1 M phosphate buffer (pH 6.5) for 72 h, strictly anaerobically, the average number of amino groups modified being 11.0, 8.8, 6.7, 6.6, 6.5, and 5.5, respectively. 

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Knowledge of the Maillard reaction is being extended very actively in many different ways. The participation of free radicals has already been dealt with in Chapter 2 and work on colour and flavour aspects is being deferred to Chapters 4 and 5, respectively. This chapter deals with a number of relatively disparate topics, namely, the effects of pH, high pressure, 7g, and the use as reactants of amines other than amino acids, of lipids, and of oligo- and polysaccharides, as well as the determination of a-dicarbonyl intermediates, control of aldol/retroaldol reactions, fluorescence, kinetic aspects, and sites of protein glycation. 

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