中文摘要：

CD147 是调停的广泛地表示的 transmembrane 蛋白质信号 transduction，和它在许多生理、病理学的过程起重要作用，例如肿瘤侵略和转移。CD147 (CD147EC ) 的细胞外的部分为它和不同发信号的分子的功能的相互作用负责。由于二张二硫化物契约的存在， CD147EC 主要在 Escherichia coli 被表示为包括身体。这里，我们报导从全部的细菌的 lysate 高效地启用 CD147EC 的 refolding 而不是纯包括身体的一个方便快速冲淡的 refolding 协议。用这个方法， CD147EC 的超过 25 mg 能在 M9 媒介从细菌的文化的 1 l 被净化。refolded CD147EC 是由原子磁性的回声(NMR ) 描绘了很好被合拢，并且它能在成纤维细胞房间导致矩阵 metalloproteinase-9 的表示。描述的协议个别地对 CD147EC 的二个免疫球蛋白领域的 refolding 也适用。有趣地，我们注意到很少蛋白质为 C 终端免疫球蛋白(Ig ) 被生产由在 M9 媒介的细菌的 CD147EC 的领域，尽管它是在 LuriaBertani (磅) 的 overexpressed 中等。然而，当在 M9 媒介的细菌的文化的 pH 在生长期间在磅媒介根据那被调整时，可比较的表示水平能被完成。

英文摘要：

CD147 is a widely expressed transmembrane protein that mediates signal transduction, and it plays important roles in many physiological and pathological processes, such as tumor invasion and metastasis. The extracellular portion of CD147 （CD147Ec） is responsible for its functional interactions with different signaling molecules. Due to the existence of two disulfide bonds, CD147Ec is mainly expressed as an inclusion body in Escherichia coli. Here, we report a convenient rapid-dilution refolding protocol that enables the refoiding of CD147EC efficiently from total bacterial lysate instead of pure inclusion bodies. Using this method, over 25 mg of CD147Ec can be purified from 1 1 of bacterial culture in M9 medium. The refolded CD147Ec is well folded as characterized by nuclear magnetic resonance （NMR）, and it can induce the expression of matrix metalloproteinase-9 in fibroblast cells. The described protocol is also applicable to the refolding of two immunoglobu-lin domains of CD147Ec individually. Interestingly, we noticed that little protein was produced for the C-terminal immunoglobulin （Ig） domain of CD147rc by bacteria in M9 medium, even though it was overexpressed in Luria-Bertani （LB） medium. However, when the pH of the bac-terial culture in M9 medium was adjusted in accordance with that in LB medium during growth, comparable expression level could be achieved.