Eschweiler B, Bohrmann B, Gerstenecker B, Schiltz E, Kist M
Institute for Medical Microbiology, Freiburg, Germany.
Zentralbl Bakteriol. 1993 Sep;280(1-2):73-85. doi: 10.1016/s0934-8840(11)80942-4.
The groEl homologue of Helicobacter pylori was isolated and characterized by means of immunoelectron microscopy, after cryosectioning. The 60 k protein was isolated from Helicobacter pylori by treatment of the cells with 2-butanol and purified by anion exchange chromatography. The native molecular weight of the 60 k protein was estimated to be 420 k by size exclusion chromatography. The purified 60 k protein showed the typical rotational symmetry of chaperonins when analyzed by electron microscopy. Ultrathin sections of Helicobacter pylori were immunostained by a polyclonal antibody directed against the hsp-65 of Mycobacterium tuberculosis. The label revealed a clustered localization of the 60 k protein on the cell surface as well as in the periplasmic space.
幽门螺杆菌的groEl同源物在冷冻切片后通过免疫电子显微镜进行分离和表征。用2-丁醇处理细胞后从幽门螺杆菌中分离出60k蛋白，并通过阴离子交换色谱法进行纯化。通过尺寸排阻色谱法估计该60k蛋白的天然分子量为420k。通过电子显微镜分析时，纯化的60k蛋白显示出伴侣蛋白典型的旋转对称性。幽门螺杆菌的超薄切片用针对结核分枝杆菌hsp-65的多克隆抗体进行免疫染色。标记显示60k蛋白在细胞表面以及周质空间呈聚集定位。
