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• W199104311 abstract "Methylglyoxal (MG), an endogenous metabolite that increases in diabetes, is a common intermediate in nonenzymatic glycation (Maillard reaction) in vivo. Here we describe the immunochemical approach to the detection of MG adducts in proteins in vitro and in atherosclerotic lesions of human aorta in vivo. The reaction of protein (bovine serum albumin) with MG led to selective loss of arginine and lysine residues, accompanied by the formation of 5‐methylimidazolone ( N δ ‐(5‐methylimidazolon‐2‐yl)ornithine) and imidazolysine (1,3‐di‐lysino‐4‐methylimidazole) derivatives, respectively. The anti‐5‐methylimidazolone antibody was prepared by immunizing rabbits with a MG‐keyhole limpet hemocyanin conjugate and purifying the serum on an affinity gel prepared by covalent attachment of the 5‐methylimidazolone derivative. The antibody cross‐reacted with the proteins treated with not only MG but trioses, such as hydroxyacetone, dihydroxyacetone, and glyceraldehyde. The immunohistochemical analysis revealed that atherosclerotic lesions of human aorta contained 5‐methylimidazolone derivatives whose distributions were identical to those of advanced glycation end products (AGEs) detected by the anti‐AGE antibody." @default.
• W199104311 created "2016-06-24" @default.
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• W199104311 date "1997-06-30" @default.
• W199104311 modified "2023-09-25" @default.
• W199104311 title "Protein modification by a Maillard reaction intermediate methylglyoxal" @default.
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• W199104311 doi "https://doi.org/10.1016/s0014-5793(97)00610-8" @default.
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