尿素对光合细菌色素蛋白复合体LH2解聚行为研究  

Effect of Urea on Depolymerization of Chlorophyll Protein Complexes from Rhodobacter sp. R7

作　　者：黄潇[1] 杨素萍[1,2] 赵春贵[1] 

机构地区：[1]山西大学化学生物学与分子工程教育部重点实验室,山西太原030006 [2]华侨大学生物技术与工程系,厦门361021

出　　处：《山西大学学报（自然科学版）》2009年第A01期143-145,共3页Journal of Shanxi University(Natural Science Edition)

基　　金：基金项目：国家自然科学基金（30470044）;太原市科技攻关（08121022）;山西省回国留学人员基金（2007）

摘　　要：采用DEAE-32纤维素柱层析、SDS-PAGE和紫外吸收光谱的方法进行Rhodobacter sp．R7菌株LH2色素蛋白复合体分离纯化、纯度测定和袁征，分离获得电泳纯的LH2色素蛋白复合体．以类胡萝卜素、细菌叶绿素特征性吸收峰为检测信号，采用紫外可见吸收光谱法研究了尿素对色素蛋白复合体解聚行为．室温下，在pH8．0 10mmol·L^-1 Tris-HCl缓冲液中，随着尿素浓度增加，LH2各特征吸收峰强度逐渐下降，峰位没有发生明显变化，也未见游离细菌叶绿素特征吸收峰．8mol／L尿素处理2h能够使LH2环状大分子解聚，但解聚后色素仍然与蛋白结合在一起，其所处的极性环境未发生明显变化，B850与B800相比细菌叶绿素B800与蛋白结合较稳定．To go deep into the study on unsolder and reconfiguration and on effect of transmission efficiency of light energy of light-harvesting complex LH2, the complex LH2 from Rhodobacter sp. R7 was separated by DEAE-32 Cellulose Column Chromatography and determined by SDS-PAGE. The infection of the urea solution concentration to light-harvesting complex LH2 was studied,with carotenoid and bacteriochloroghyll as detection signal by UV Vis absorption spectroscopy. The strength of characteristic absorption peak of LH2 descended as the concentration of urea ascended in Tris-HCl buffer （pH 8.0 10 mmol ·L^-1） at room temperature, and the peak position changed little. The peak position of dissociative bacteriochlorophyll was not detected while urea solution concentration at 8mol/L. So the light-harvesting complex LH2 was depolymerized by 8 mol/L urea solution for 2 hours, but the pigment still combined with protein and its polar surroundings changed unconspicuous. Compared to B850,bacteriochlorophyll B800 combined with protein more stably.

关 键 词：光合细菌 色素蛋白复合体 尿素 

分 类 号：Q819[生物学—生物工程] Q939