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机构地区:[1]第四军医大学唐都医院眼科,陕西西安710033 [2]第四军医大学西京医院理疗科,陕西西安710033
出 处:《第四军医大学学报》2002年第12期1071-1073,共3页Journal of the Fourth Military Medical University
基 金:"十五"全军指令性课题 (0 1L0 71)
摘 要:目的 探讨次声对 α-晶体蛋白分子伴侣活性的影响 .方法 采用 Sephacryl S- 30 0凝胶柱分离牛α-晶体蛋白 .应用次声压力舱 ,以 16 Hz,130 d B次声作用 αL-晶体蛋白溶液 (g· L- 1 ) ,每天作用 2 h,连续 16 d.分光光度计检测 36 0nm时αL-晶体蛋白对加热诱导过氧化氢酶 (CAT)和βL-晶体蛋白凝聚的保护作用 .孵育 6 0 min,以 αL-晶体蛋白占对照靶蛋白光散射值的百分比表示α-晶体蛋白分子伴侣功能 .结果 与对照蛋白比较 ,α-晶体蛋白具有特异性保护 CAT和 βL-晶体蛋白热凝聚的作用 .次声作用第 16日 ,对照组 αL-晶体蛋白保护 βL-晶体蛋白热凝聚的作用为 (92 .0± 3.1) % ,次声组为 (81.2± 5 .4 ) % ,降低约 10 .8% (P<0 .0 1) ;对照组 αL-晶体蛋白保护 CAT热凝聚的作用为 (73.8± 5 .1) % ,次声组为(6 1.8± 9.1) % ,降低约 12 .0 % (P<0 .0 1) .AIM To investigate the effect of infrasound on molecular chaperone activity of α crystallin. METHODS The α crystallin of bovine lens were separated by chromatography on Sephacryl S 300 HR. The solutions of α L crystallin (mg·ml -1 ) from nucleus were exposed to infrasound of 16 Hz with the intensity of 160 dB (2 hours per day for 16 consecutive days). The protective effects of α L crystallin on thermal aggregation of catalase and β L crystallin were measured spectrophotometrically at 360 nm. The chaperone activity of α crystallin was represented as the percentage of protection by α L crystallin of the scattering produced by the target protein control after 60 min incubation. RESULTS α L Crystallin specifically protected catalase and β L crystallin against thermal aggregation compared with control proteins. At 16 days after exposure to infrasound, protection catalase against thermal aggregation in infrasound group (73.8±5.1%) was decreased by 12% comparing with control group (61.8± 9.1%) ( P <0.01), and protection β L crystallin against thermal aggregation in infrasound group (81.2±5.4%) was by 10.8% comparing with control group (92.0±3.1%)( P < 0.01). CONCLUSION These results suggest that infrasound can influence the molecular chaperone activity of α crystallin.
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