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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 .
Objective To study chaperone characteristics of α-crystallin.Methods Sephacryl S-30 0 HR gel column was used to separate and purify bovine α-crystallins Protein.The activity of superoxide dismutase (SOD) and catalase (CAT) were detected by spectrophotometer, and the activity of α-crystal protein was expressed as a percentage of the activity of the control group retained by enzyme inactivation Results The incubation of carbohydrates with enzymes resulted in the inactivation of time-dependent SOD and CAT, and the rapid inactivation of glycosylation induced by both fructose and ribose compared to 6-phosphoglucose and glucose resulted in the rapid inactivation of SOD and CAT.α-crystallin compared with control protein , With specific protection against glycosylation-induced inactivation of SOD and CAT.Conclusion This result further supports the alpha-crystallin molecular chaperone activity that protects the enzyme from inactivation.