摘要
目的:研究硒性白内障α-晶体蛋白的分子伴侣特性。方法:制作SD大鼠亚硒酸钠性白内障模型,分离纯化正常和白内障晶状体α-晶体蛋白。观察α-晶体蛋白对过氧化氢酶（CAT）热凝聚的抑制作用。结果:正常和硒性白内障幼鼠晶状体α-晶体蛋白与对照蛋白比较,具有特异性抑制CAT热凝聚的作用;αH较αL-晶体蛋白伴侣功能降低;硒性白内障α-晶体蛋白的抑制作用下降,正常和白内障晶状体αH和αL-晶体蛋白伴侣功能两者之间分别比较均有显著性差异。结论:硒性白内障α-晶体蛋白抑制CAT热凝聚的分子伴侣活性下降是导致白内障形成的重要环节。眼科学报2001;17:78～81。
Purpose: To evaluate the character of a-crystallin molecular chaperone activity in selen-ite cataract.Methods: α-Crystallin from lenses of normal young rats and lenses with selenite cataract were separated and purified by gel filtration chromatography. The chaperone activity of a-crystallin was assayed by mearsuring heat-induced aggregation and scattering of cata-lase.Results: α-Crystallin in both normal and cataractous lenses specifically prevented cata-lase against thermal aggregation compared with control proteins. The preventive ability in otH-crystallin was less than in otL-crystallin. Chaperone activity was diminished in selenite cataract. There was statistically significant difference in chaperone activity between normal and cataractous lenses in both an-crystallin and ai.-crystallin respectively. Conclusion: The reduction of a-crystallin chaperone activity in selenite cataract by preventing thermal aggregation of catalase is an important process in cataract formation. Eye Science 2001; 17: 78 - 81.
出处
《眼科学报》
2001年第2期78-81,共4页
Eye Science
基金
中国人民解放军总后勤部卫生部留学回国人员基金资助(No:97H26)
