论文部分内容阅读
为了研究IL-6生物活性与蛋白质结构的关系,以及与活性有关的结构是否具有细胞特异性,建立了三组变异株:(1)rIL-6S变异株,4个天然存在的半胱氨酸被丝氨酸所取代;(2)在含有半胱氨酸的IL-6分子中建立一系列变异株,每个变异株内部都有40个氨基酸的缺失,这样在人类IL-6分子184个氨基酸中建立了一系列从N 端第4到第183氨基酸彼此相互连接的缺失变异株(rIL-6_(△4-23),rIL-6_(△24-43…));(3)在不含半胱氨酸的IL-6中第4～23氨基酸的缺失(rIL-6S_(△4-23))。然后用小鼠杂交细胞瘤增殖、EB 病毒转化人B 细胞系IgM的分泌、大鼠肝细胞纤维蛋白原分泌以及人类肝细胞纤维蛋白原分泌等试验来分析每种变异株的变异与活性的关系。
In order to study the relationship between the biological activity of IL-6 and the protein structure and whether the structure related to the activity is cell-specific, three groups of mutants were established: (1) rIL-6S mutant, four naturally occurring cysteines Is replaced by serine; (2) a series of mutant strains are established in the cysteine-containing IL-6 molecule, and each of the mutant strains has a deletion of 40 amino acids inside, so that in 184 amino acids of human IL-6 molecule A series of deletion mutants (rIL-6_ (△ 4-23), rIL-6_ (△ 24-43 ...)) were constructed which were connected to the 4th through the 183th amino acids of N terminal. (3) The deletion of the 4th to 23th amino acids in IL-6 of cystine (rIL-6S_ (Δ4-23)). Then, the relationship between the variation and the activity of each mutant was analyzed by the proliferation of mouse hybridoma, the secretion of Epstein-Barr virus-transformed human B cell line IgM, the secretion of fibrinogen in rat hepatocytes and the secretion of fibrinogen in human hepatocytes .