Faculty of Chemistry, University of Wrocław, 50-137 Wrocław, Poland.
Biochem Biophys Res Commun. 2013 Sep 13;439(1):78-83. doi: 10.1016/j.bbrc.2013.08.025. Epub 2013 Aug 16.
Although in vivo glycation proceeds in complex mixture of proteins, previous studies did not take in consideration the influence of protein-protein interaction on Maillard reaction. The aim of our study was to test the influence of human serum albumin (HSA) on glycation of fibrinogen. The isotopic labeling using [(13)C6] glucose combined with LC-MS were applied as tool for identification possible glycation sites in fibrinogen and for evaluation the effect of HSA on the glycation level of selected amino acids in fibrinogen. The obtained data indicate that the addition of HSA protects the fibrinogen from glycation. The level of glycation in presence of HSA is reduced by 30-60% and depends on the location of glycated residue in sequence of protein.
尽管体内糖化是在蛋白质的复杂混合物中进行的，但之前的研究并未考虑蛋白质-蛋白质相互作用对美拉德反应的影响。我们的研究目的是测试人血清白蛋白 (HSA) 对纤维蛋白原糖化的影响。使用 [(13)C6] 葡萄糖的同位素标记结合 LC-MS 被用作鉴定纤维蛋白原中可能的糖化位点的工具，并评估 HSA 对纤维蛋白原中选定氨基酸糖化水平的影响。所得数据表明，HSA 的添加可保护纤维蛋白原免受糖化。在存在 HSA 的情况下，糖化水平降低了 30-60%，并且取决于糖化残基在蛋白质序列中的位置。
