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Association of adenovirus early-region 1A proteins with cellular polypeptides.

机译:腺病毒早期区域1A蛋白与细胞多肽的关联。

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Extracts from adenovirus-transformed human 293 cells were immunoprecipitated with monoclonal antibodies specific for the early-region 1A (E1A) proteins. In addition to the E1A polypeptides, these antibodies precipitated a series of proteins with relative molecular weights of 28,000, 40,000, 50,000, 60,000, 80,000, 90,000, 110,000, 130,000, and 300,000. The two most abundant of these polypeptides are the 110,000-molecular-weight protein (110K protein) and 300K protein. Three experimental approaches have suggested that the 110K and 300K polypeptides are precipitated because they form stable complexes with the E1A proteins. The 110K and 300K polypeptides do not share epitopes with the E1A proteins, they copurify with a subset of the E1A proteins, and they bind to the E1A proteins following mixing in vitro. The 110K and 300K polypeptides are not adenoviral proteins, but are encoded by cellular DNA. Both the 12S and the 13S E1A proteins bind to the 110K and 300K species, and these complexes are found in adenovirus-transformed and -infected cells.
机译:用特异于早期1A(E1A)蛋白的单克隆抗体免疫沉淀来自腺病毒转化的人293细胞的提取物。除了E1A多肽外,这些抗体还沉淀了一系列蛋白质,相对分子量分别为28,000、40,000、50,000、60,000、80,000、90,000、110,000、130,000和300,000。这些多肽中最丰富的两个是110,000分子量蛋白质(110K蛋白质)和300K蛋白质。三种实验方法表明110K和300K多肽会沉淀,因为它们与E1A蛋白形成稳定的复合物。 110K和300K多肽与E1A蛋白不共享表位,它们与一部分E1A蛋白共纯化,并且在体外混合后与E1A蛋白结合。 110K和300K多肽不是腺病毒蛋白,但由细胞DNA编码。 12S和13S E1A蛋白都与110K和300K物种结合,并且这些复合物在腺病毒转化和感染的细胞中发现。

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