摘要
目的了解兔α－晶状体蛋白是否具有分子伴娘功能。方法凝胶过滤法分离水溶性晶状体蛋白。在５５℃高温条件下，观察。一晶状体蛋白是否能抑制β－ｌｏｗ晶状体蛋白的凝集和变性；观察α－晶状体蛋白是否能抑制糖基化诱导的葡萄糖－６－磷酸脱氢酶（Ｇ６ＰＤ）的失活，均以牛血清白蛋白（ＢＳＡ）作为对照。结果α－晶状体蛋白能抑制热诱导的β－ｌｏｗ晶状体蛋白的凝集和变性；α－晶状体蛋白亦能抑制糖基化诱导的Ｇ６ＰＤ的失活；而牛血清白蛋白却无此作用。结论α－晶状体蛋白具有分子伴娘功能。
Objective To study whether α-crystalline has function of a molecular chaperone. Methods (1) The watersoluble crystalline of rabbits was purified by Sephadex G-200 gel filtration. (2 ) The cuvettes were heated to 55t for 8-low crystalline aggregation,in some cuvettes ac-crystalline were added, the scattering resulting from aggregation was measured continuously by spectrophotometer at 360 urn. Observe whether a-crystalline can prevent thermal aggregation of p-low crystalline. Bovine serum albumin(BSA) was employed as control. (3 ) Fructose incubated by glucose-6-phosphate dehydrogenase for 0, l, 2 and 3 h at 37℃. In some experiments, a-crystalline and bovine serum albumin were added to different vials during incubation. Enzyme activity was assayed by monitoring the increased absorbance at 340 nm for 5 min,activity was expressed relative to the activity for each incubation mixture at 0 time, Observe whether α-crystalline could prevent sugar inactivity of glucose-6-phosphate dehydrogenase. Results The a-crystalline could prevent thermal aggregation of p-low crystalline and protect from glycation-induced inactivity of glucose-6-phosphate dehydrogenase, but bovine serum albumin could not. Conclusion The α-crystalline has function of a molecular chaperone.
出处
《眼科研究》
CSCD
北大核心
2001年第3期211-213,共3页
Chinese Ophthalmic Research
基金
云南省教委科研基金资助(资助号:9911011)
