Dicarbonyl compounds react more rapidly, than glucose, with arginine and lysine in proteins to form advanced glycation end products (AGEs) and further produce free radicals which cause DNA damage. AGEs are reliable diagnostic biomarkers for most of the age-related diseases. In the present study histone was modified with glyoxal and it was characterized by various spectral techniques. Binding characteristics of the modified histone towards serum antibodies from type 1 diabetes patients was evaluated by solid phase enzyme immunoassay and the results were compared with normal human subjects. Fluorescence and Fourier transformed infrared analysis of the nuclear protein clearly indicated changes in their respective intensities upon modification with glyoxal. Liquid chromatography together with mass spectrometry showed new peaks and m/z values related to AGE adducts of dihydroimidazolidines/hydroimidazolones. This glyoxal modified protein was recognized by serum antibodies of the diabetes patients while it showed negligible binding with that of normal human subjects. Glyoxal modification of histone causes structural turbulence and formation of advanced glycation adducts in histone. These adducts might be the main antigenic epitope of the modified histone, leading to its recognition by circulating type 1 diabetes antibodies.

中文翻译：

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乙二醛对组蛋白的修饰作用：1型糖尿病患者血清抗体识别含晚期糖基化加合物的糖化组蛋白

与葡萄糖相比，二羰基化合物与蛋白质中的精氨酸和赖氨酸反应更快，形成高级糖基化终产物（AGEs），并进一步产生导致DNA损伤的自由基。AGEs是大多数与年龄有关的疾病的可靠诊断生物标志物。在本研究中，用乙二醛修饰了组蛋白，并通过各种光谱技术对其进行了表征。通过固相酶免疫测定法评估了修饰的组蛋白与1型糖尿病患者血清抗体的结合特征，并将结果与​​正常人进行了比较。核蛋白的荧光和傅里叶变换红外分析清楚地表明了乙二醛修饰后它们各自强度的变化。液相色谱和质谱联用显示了新的峰和m / z值与二氢咪唑烷/氢咪唑啉酮的AGE加合物有关。这种乙二醛修饰的蛋白被糖尿病患者的血清抗体识别，而与正常人的结合却可忽略不计。组蛋白的乙二醛修饰会导致结构紊乱并在组蛋白中形成高级糖基化加合物。这些加合物可能是修饰组蛋白的主要抗原表位，导致其被循环1型糖尿病抗体识别。