Characterization of the particles produced by exposure of ribosomal subunits to urea.
When Escherichia coli 50-S ribosomal subunits are treated with increasing concentrations of urea partial deproteination occurs. Furthermore, we observed that the number of sulfhydryl groups which react with Ellman's reagent is a sigmoidal function of the urea concentration. These results are similar to those previously reported for the 30-S subunit (Acharya, A.S. and Moore, P.B. (1973) J. Mol. Biol. 76, 207-221). For both subunits we identify the proteins which dissociate (split proteins) or are recoverable in a ribonucleoprotein particle (core proteins) under the action of 6 M urea in a buffer of moderate ionic strength.
D001426:Bacterial Proteins / Q000032:analysis; D001665:Binding Sites; D004228:Dithionitrobenzoic Acid; D004926:Escherichia coli / Q000648:ultrastructure; D011485:Protein Binding; D012270:Ribosomes / Q000187:drug effects / Q000648:ultrastructure*; D014508:Urea / Q000494:pharmacology*
D001426:Bacterial Proteins; D014508:Urea; D004228:Dithionitrobenzoic Acid