Marcantonio E E, Grebenau R C, Sabatini D D, Kreibich G
Eur J Biochem. 1982 May;124(1):217-22. doi: 10.1111/j.1432-1033.1982.tb05928.x.
Microsomes prepared from several animal sources were analyzed for the presence of proteins corresponding to the ribophorins (I and II) which have been previously characterized in rat liver rough microsomes and appear to be involved in the binding of polysomes to endoplasmic reticulum membranes. In rough microsomal membranes from rat lacrimal gland, rabbit liver, dog and chicken pancreas, and mouse myeloma, ribophorin-like polypeptides with similar electrophoretic mobilities were detected by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. In all cases the polypeptides remained associated with sedimentable polysomes after solubilization of the microsomal membranes with nonionic detergents. Ribophorin-like polypeptides were absent from smooth microsomes. Antibodies raised against each rat liver ribophorin, purified by preparative sodium dodecyl sulfate/polyacrylamide gel electrophoresis, immunoprecipitated only the corresponding polypeptide, indicating no crossreactivity between ribophorins I and II. These antibodies also immunoprecipitated the homologous ribophorins found in microsomal preparations from other organs and species.
对从多种动物来源制备的微粒体进行了分析，以检测是否存在与核糖体结合蛋白（I和II）相对应的蛋白质，核糖体结合蛋白先前已在大鼠肝脏粗面微粒体中得到表征，似乎参与多核糖体与内质网膜的结合。在大鼠泪腺、兔肝脏、狗和鸡胰腺以及小鼠骨髓瘤的粗面微粒体膜中，通过十二烷基硫酸钠/聚丙烯酰胺凝胶电泳检测到具有相似电泳迁移率的核糖体结合蛋白样多肽。在所有情况下，在用非离子去污剂溶解微粒体膜后，这些多肽仍与可沉降的多核糖体相关联。滑面微粒体中不存在核糖体结合蛋白样多肽。通过制备性十二烷基硫酸钠/聚丙烯酰胺凝胶电泳纯化的针对每种大鼠肝脏核糖体结合蛋白产生的抗体，仅免疫沉淀相应的多肽，表明核糖体结合蛋白I和II之间没有交叉反应。这些抗体还免疫沉淀了在来自其他器官和物种的微粒体制备物中发现的同源核糖体结合蛋白。
