摘要
α-晶体蛋白 ;分子伴侣 ;超氧化物歧化酶 ;过氧化氢酶 ;糖基化目的 研究 α-晶体蛋白的分子伴侣特性 .方法 采用 Sephacryl S-30 0 HR凝胶柱分离纯化牛α-晶体蛋白 .应用分光光度计检测超氧化物歧化酶 ( SOD)和过氧化氢酶 ( CAT)的活性 ,以酶失活后保留的酶活性占其对照组活性的百分比表示 α-晶体蛋白的伴侣作用 .结果 糖与酶的孵育导致时间依赖性的 SOD和 CAT失活 .果糖和核糖比 6-磷酸葡萄糖和葡萄糖具有糖基化诱导 SOD和 CAT的快速失活效应 .α-晶体蛋白与对照蛋白比较 ,具有特异性保护糖基化诱导 SOD和CAT的失活 .结论 本结果进一步支持 α-晶体蛋白具有分子伴侣活性 ,可保护酶的失活 .
AIM To investigate the chaperone like properties of α crystallin. METHODS α crystallin of bovine lens was isolated and purified by Sephacryl S 300 HR gel filtration column. The activities of superoxide dismutase and catalase were measured with a spectrophotometer. The chaperone like properties of α crystallin were represented as the percentage activity remaining of enzymes compared with the corresponding incubation of its control. RESULTS Incubation with sugars resulted in a time dependent inactivation of the enzymes. Fructose and ribose inactivated them more rapidly than glucose 6 phosphate and glucose. α crystallin specifically protected antioxidant enzymes against glycation induced inactivation compared with control proteins. CONCLUSION These results further support the view that α crystallin acts as molecular chaperone and protects against inactivation of enzymes.
出处
《第四军医大学学报》
2000年第11期1352-1354,共3页
Journal of the Fourth Military Medical University
