- 作者: 黃福永 ; 何愈 ; 許銘清 ; 翁鳳如
- 作者服務機構: 成功大學化學系
- 中文摘要: Raman vibrations of the fingerprint of aromatic amino acid residues were analyzed to study the changes of cataractous lens protein in the cortex and nucleus at various ages. Tryptophan content, analyzed by the quantification of I/sub 758//I/sub 1448/ ratio, shows the damage(modification) of tryptophan residue in the nucleus is caused primarily by the formation of cataracts, not by the aging process. Microenvironmental changes of tryptophan and tyrosine were analyzed by the intensity ratios of I/ sub 879//I/sub 758/ and I/sub 829//I/sub 853/, respectively. The decrease of the ratio of I/sub 879//I/sub 758/, from 0.9 to 0.6 in the nucleus and from 0.7 to 0.6 for the cortex, reveal that more buried tryptophan residues become exposed in the cortex than in the nucleus during cataractogenesis, especially for non-senile cataractous lenses. The ratio of I/sub 829//I/sub 853/ is around 1.0 for both cortical and nuclear proteins at various ages, indicating some tyrosine residues have undergone a change in their hydrogen bonding environment. When compared to previous studies, we found that a normal (clear) lens has a higher peak at 1617cm/sup -1/ than at 1604cm/sup -1/, while a dense opaque or brunescent lens shows stronger intensity at 1604cm/sup -1/ than at 1617cm/sup -1/, suggesting the ratio of I/sub 1617//I/sub 1604/ can be used to evaluate the human lens morphology.
- 英文摘要: --
- 中文關鍵字: Near Infrared Fourier Transform Raman Spectroscopy; Cataractous Lens
- 英文關鍵字: 近紅外線傅立葉轉移拉曼光譜;白內障