Liang J N, Rossi M T
Howe Laboratory of Ophthalmology, Massachusetts Eye and Ear Infirmary, Harvard Medical School, Boston 02114.
Exp Eye Res. 1990 Apr;50(4):367-71. doi: 10.1016/0014-4835(90)90137-j.
Calf lens LMW alpha-crystallin was glycated by incubating with various sugars (glucose, glucose-6-P and ribose) for 21 days. All sugars induced disulfide formation, but ribose also produced higher molecular weight cross-linked species. The ribocated protein turned yellow in color and had a strong blue fluorescence (Ex/Em = 370/450 nm) typical for a browning product. The chromophore of the browning product showed a new circular dichroism (CD) band at 320-330 nm. Conformational study indicated that the browning reaction destablized protein and may play a significant role in protein aggregation and insolubilization.
通过与各种糖类（葡萄糖、6-磷酸葡萄糖和核糖）孵育21天，使小牛晶状体低分子量α-晶状体蛋白发生糖基化。所有糖类均诱导二硫键形成，但核糖还产生了更高分子量的交联产物。核糖糖化的蛋白质变为黄色，并具有典型褐变产物的强烈蓝色荧光（激发波长/发射波长 = 370/450 nm）。褐变产物的发色团在320 - 330 nm处显示出一条新的圆二色性（CD）带。构象研究表明，褐变反应使蛋白质不稳定，可能在蛋白质聚集和不溶性形成中起重要作用。
