本實驗利用蛋白質體學的分析技術對餵食半乳糖誘使產生白內障的大白鼠之水晶體作研究，得到結果如下：由快速蛋白質液相層析儀分析水晶體內的水溶性水晶體蛋白，發現隨著得到白內障的時間增長大白鼠水晶體內的β水晶體蛋白和γ水晶體蛋白明顯的減少。另外，尿素可溶性蛋白中主要的成份β-A3、β-B1和β-B3的多胜肽片段出現被修飾的情形，如組胺酸(Histidine)、色胺酸(Tryptophan)、甲硫胺酸(Methionine)被氧化(Oxidation)、丙胺酸(Alanine)接有乙醯基、親水性的半胱胺酸(Cysteine)出現Oxalate Monoalkylamide，而水溶性蛋白成分中的β-A3、β-B1和β-B3多肽片段也有被氧化、乙醯化，但沒有出現Oxalate Monoalkylamide的修飾，這個差異可能就是造成β-A3、β-B1和β-B3水晶體蛋白從水溶性蛋白質變化成非水溶性蛋白質的原因之一，而這些蛋白質受到的修飾可能讓水晶體蛋白聚集形成非水溶性蛋白質造成水晶體混濁。

Both proteomics and LC-MS/MS have been used to intensively investigate the protein post translation. In this study, two-dimensional gel electrophoresis followed by LC-MS/MS analysis have been employed to study the protein glycation of galactosemic cataract rat lenses. It was found that after feeding galactose, the rat lens started to show cortical nucleus cataract at week three. And the water soluble fraction of the lens showed that the contents of βH and γ crystallins decrease significantly with the increase of feeding time. It was also found that β-A3、β-B1 and β-B3crystallin in urea soluble fraction of the cataract lens had undergone oxidative modification at Histidine, Trptopha, and Methionien residues, acetylation at Alanine residue, and oxalate monoalkylamide modification at Cysteine residue. Interestingly, the water soluble fraction of cataract rat lens also underwent oxidation and acetylation; however, no oxalate monoalkylamide modification was observed for β-A3、β-B1 and β-B3 crystallin. The difference in oxalate monoalkylamide modification in water soluble fraction may suggest that this modification is the main cause to cause the denaturation of rat lens crystallins as to cause the formation of cataract.

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