Schenkel J, Hovemann B
Institut für Immunologie, Universität, Heidelberg, FRG.
Biochem Biophys Res Commun. 1990 Mar 30;167(3):1196-9. doi: 10.1016/0006-291x(90)90650-c.
A polyclonal antiserum against purified bacteriophage T4 gene 32 protein was raised in rabbits. In Western blots it detected a number of SDS-PAGE separated nuclear and ribosomal proteins of HeLa cells. Using a renaturing blotting system, however, larger hnRNP proteins ranging between 66.000 and 82.000 Da preferentially reacted with this antiserum. In addition hnRNP group A core proteins were detected to a minor extent. Nucleic acid binding proteins like histones or ribosomal proteins were not stained by this antibody after renaturation.
针对纯化的噬菌体T4基因32蛋白制备了兔多克隆抗血清。在蛋白质免疫印迹中,它检测到一些经SDS-PAGE分离的HeLa细胞核蛋白和核糖体蛋白。然而,使用复性印迹系统时,分子量在66,000至82,000道尔顿之间的较大hnRNP蛋白优先与该抗血清发生反应。此外,还在较小程度上检测到hnRNP A组核心蛋白。复性后,组蛋白或核糖体蛋白等核酸结合蛋白不会被该抗体染色。