CAJ | 학술논문

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α-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
목적　료해토α-정상체단백시부구유분자반낭공능。방법　응효과려법분리수용성정상체단백재55℃고온조건하,관찰α-정상체단백시부능억제β-low정상체단백적응집화변성;관찰α-정상체단백시부능억제당기화유도적포도당-6-린산탈경매(G6PD)적실활,균이우혈청백단백(BSA)작위대조。결과　α-정상체단백능억제열유도적β-low정상체단백적응집화변성;α-정상체단백역능억제당기화유도적G6PD적실활;이우혈청백단백각무차작용。결론　　α-정상체단백구유분자반낭공능
ObjectiveTo study whether α-crystalline has function of a molecular chaperone.Methods(1)The water-soluble crystalline of rabbits was purified by Sephadex G-200 gel filtration.(2)The cuvettes were heated to 55℃ for β-low crystalline aggregation,in some cuvettes α-crystalline were added,the scattering resulting from aggregation was measured continuously by spectrophotometer at 360 nm.Observe whether α-crystalline can prevent thermal aggregation of β-low crystalline.Bovine serum albumin(BSA) was employed as control.(3)Fructose incubated by glucose-6-phosphate dehydrogenase for 0,1,2 and 3 h at 37℃.In some experiments,α-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.　ResultsThe α-crystalline could prevent thermal aggregation of β-low crystalline and protect from glycation-induced inactivity of glucose-6-phosphate dehydrogenase,but bovine serum albumin could not.ConclusionThe α-crystalline has function of a molecular chaperone