Lapolla Annunziata, Fedele Domenico, Senesi Antonella, Arico Nadia Concetta, Reitano Rachele, Seraglia Roberta, Astner Hubert, Traldi Pietro
Farmaco. 2002 Oct;57(10):845-52. doi: 10.1016/s0014-827x(02)01305-8.
An investigation on AGE-peptides, originating by proteolysis of in vitro glycated proteins, was carried out by LC methods with different detection applied to the mixture produced by proteinase K digestion of in vitro glycated human serum albumin (HSA). Classical approaches, like spectroscopic (UV, fluorescence) and mass spectrometric methods (MALDI, LC/ESI/MS), show that the digestion mixture is highly complex. However, there are clearcut differences between the digestion mixtures of glycated and unglycated HSA, in the former case allowing identification of possible glycated peptides belonging to the AGE-peptide class. MS/ MS experiments on selected species seem to be promising as regards structural information.
通过液相色谱（LC）方法，采用不同的检测手段，对体外糖化蛋白质经蛋白水解产生的晚期糖基化终末产物（AGE）肽进行了研究，该研究应用于体外糖化人血清白蛋白（HSA）经蛋白酶K消化产生的混合物。传统方法，如光谱法（紫外、荧光）和质谱法（基质辅助激光解吸电离、液相色谱/电喷雾电离/质谱），表明消化混合物高度复杂。然而，糖化和未糖化HSA的消化混合物之间存在明显差异，在前一种情况下，可以鉴定出可能属于AGE肽类的糖化肽。对选定物种进行的串联质谱（MS/MS）实验在获取结构信息方面似乎很有前景。
