关键词: α-晶体蛋白;分子伴侣;次声

    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-300凝胶柱分离牛α-晶体蛋白.应用次声压力舱，以16Hz，130dB次声作用αL -晶体蛋白溶液(g·L-1 )，每天作用2h，连续16d.分光光度计检测360nm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60min，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<0.01);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(61.8±9.1)%，降低约12.0%(P<0.01). 结论 次声可影响α-晶体蛋白的分子伴侣活性.

    Effect of infrasound on molecular chaperone activi┐ty ofα┐crystallin

    YAN Hong CHENG Jing-Zao JIA Ke-Yong

    1 Department of Ophthalmology，Tangdu Hospital，

    2 Department of Rehibility&Physiotherapy，Xijing Hospital，Fourth Military Medical University，Xi'an710033，China

    Keywords:α-crystallin;molecular chaperone;infrasound

    Abstract:AIM To investigate the effect of infrasound on molecular chaperone activity ofα-crystallin.METHODS Theα-crystallin of bovine lens were separated by chromatog-raphy on Sephacryl S-300HR.The solutions ofαL -crystallin(mg·ml-1 )from nucleus were exposed to infrasound of16Hz with the intensity of160dB(2hours per day for16con-secutive days).The protective effects ofαL -crystallin on ther-mal aggregation of catalase andβL -crystallin were measured spectrophotometrically at360nm.The chaperone activity ofα-crystallin was represented as the percentage of protection byαL -crystallin of the scattering produced by the target pro-tein control after60min incubation.RESULTS αL -Crys-tallin specifically protected catalase andβL -crystallin against thermal aggregation compared with control proteins.At16days after exposure to infrasound ......