Open AccessSensitive Separation Procedure for Escherichia coli Ribosomal Proteins and the Resolution of High‐Molecular‐Weight Components
Author(s) -
Subramanian Alap R.
Publication year - 1974
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1974.tb03579.x
Subject(s) - ribosomal protein , ribosome , escherichia coli , resolution (logic) , protein subunit , polyacrylamide gel electrophoresis , ribosomal rna , high resolution , polyacrylamide , chemistry , chromatography , electrophoresis , biochemistry , biology , microbiology and biotechnology , rna , enzyme , gene , computer science , artificial intelligence , remote sensing , geology
Application of the two‐dimensional polyacrylamide gel electrophoretic procedure recently described by Mets and Bogorad [4] to the resolution of Escherichia coli ribosomal proteins is described. This procedure is fast (running time of 8–10 h) and highly sensitive (1–2 μg protein per spot) and it gave good resolution for the majority of the 55 proteins in E. coli ribosomes. Moreover, the method has permitted the resolution of a large number of high‐molecular‐weight proteins associated with ribosomes not exposed to high‐salt washing. Using purified proteins, the positions in the electrophrogram of the individual proteins of the 30–S subunit have been determined.