Mota M C, Carvalho P, Ramalho J S, Cardoso E, Gaspar A M, Abreu G
Center for Ophthalmology, University of Coimbra, Portugal.
Int Ophthalmol. 1994;18(4):187-93. doi: 10.1007/BF00951795.
Glycated proteins formed by the Maillard reaction were measured by furosine determination in human normal lenses and in senile and diabetic cataracts. Furosine, an hydrolysis product of fructose-lysine adduct formed in the early stages of the Maillard reaction, was measured by high performance liquid chromatography (HPLC). Furosine levels in diabetic cataracts were found to be 3 to 4 times higher than those observed for senile cataracts. The increased glycation levels both in cortex and nucleus were related to the increase of fluorescence determined in vitro by fluorometry and in vivo by Scheimpflug photography. Lens proteins were incubated with glucose and it has been demonstrated that protein glycation occurred parallel with the increase in concentration of fluorescent chromophores that present similar characteristics as those observed in vivo. The results indicate that protein insolubilization seemed to involve preferentially glycated proteins and at least in diabetic cataracts, the process seems to be initiated in the cortical region.
通过测定人正常晶状体、老年性白内障和糖尿病性白内障中的糠氨酸来检测美拉德反应形成的糖化蛋白。糠氨酸是美拉德反应早期形成的果糖 - 赖氨酸加合物的水解产物，通过高效液相色谱法（HPLC）进行测定。发现糖尿病性白内障中的糠氨酸水平比老年性白内障中观察到的水平高3至4倍。皮质和核中糖化水平的增加与体外荧光法和体内Scheimpflug摄影法测定的荧光增加有关。晶状体蛋白与葡萄糖一起孵育，结果表明蛋白质糖化与荧光发色团浓度的增加同时发生，这些荧光发色团具有与体内观察到的相似特征。结果表明，蛋白质不溶性似乎优先涉及糖化蛋白，至少在糖尿病性白内障中，该过程似乎始于皮质区域。
