作者: H M Olson , A Sommer , D S Tewari , R R Traut , D G Glitz
DOI: 10.1016/S0021-9258(19)62705-5
关键词: Protein subunit 、 Immunoelectron microscopy 、 Molecular biology 、 Epitope 、 Large ribosomal subunit 、 Biology 、 Ribosome 、 Ribosomal RNA 、 Ribosomal protein 、 Monoclonal antibody 、 Cell biology 、 Biochemistry
摘要: Four molecules of ribosomal protein L7/L12 are found as two dimers on the Escherichia coli 50 S subunit. Immune electron microscopy using monoclonal antibodies directed against epitopes has allowed placement elements each dimer. One antibody, a determinant in COOH-terminal domain, allows localization identical determinants at or near end subunit stalk. The same antibody was used to place additional periphery stalkless subunits, an area from which stalk might be expected project. A second epitope amino-terminal portion L7/L12, caused loss stalks subunits. micrographs showed symmetrical oligometric complexes dissociated dimeric with bivalent antibody. Antibodies were also seen bind body region sites. results explained by model one dimer exists folded conformation and occurs extended