RAMAN SPECTROSCOPIC INVESTIGATION OF LENS AGING & CATARACT FORMATION

这项研究的目的是调查白内障 用拉曼光谱研究眼晶状体的形成和老化。它是有的 有人提出晶状体晶状体蛋白的氧化会导致二硫化物 蛋白质构象中的交联和相关变化是 Moajor参与晶状体老化和白内障的形成。我们已经获得了 天然伽马II晶体单体和二聚体的拉曼光谱 形态用高效液相色谱测定，对照样品。拉曼光谱 在511 cm-1处检测到二硫化物的形成(S-S)。我们跟随着 S-S亮相后晶体蛋白的氧化 511厘米-1频率和S-H频率在2500-2600附近消失 Cm-1。初步的拉曼结果还表明，二硫化物 形成或氧化不会导致显著的变化 蛋白质的二级构象。目前我们正在尝试 确定二硫化物交联物是分子内的还是 分子间的相互作用，并估计这一比例，如果是由于两者。

The objective of this research is to investigate the cataract formation and aging of eye lens using Raman spectroscopy. It is has been proposed that oxidation of lens crystallins leading to disulfide cross linking and associated changes in protein conformation are moajor steps in lens aging anf cataract formation. We have obtained Raman spectra of native gamma II crystallin in monomer form and dimer form determined by HPLC, and control samples. Raman spectroscopy detected disulfide formation (S-S) at 511 cm-1. We followed the oxidation of crystallin protein by following the appearance of S-S frequency at 511 cm-1 and disappearance S-H frequency near 2500-2600 cm-1. The initial Raman results also suggested that disulfide formation or oxidation does not result in significant changes in secondary conformation of the protein. Currently we are trying determine whether the di-sulfide cross linking is intramolecular or inter molecular and estimate the ratio if it is due to both.