We have investigated the protein-protein cross-links formed within the 60 S subunit of the Escherichia coli ribosome using 2-iminothiolane as the cross-linking reagent.The members of the cross-links have been identified by immunoblotting from one-dimensional and two-dimensional diagonal sodium dodecyl sulfatepolyacrylamide gels using antisera specific for the individual ribosomal proteins.This method also allowed a quantitation of the yield of cross-linking for each cross-link.A total of 14 cross-links have been identified Ll-L33, L2-L9, L2-LS-L28, L3-Ll9, L9-L28, L19-L25, L20-L21, L22-L32, and L23-L34.Our results are compared with those of Traut and coworkers (Traut, R.
No takes yet. Share an insight, caveat, or question.
Walleczek et al. (1989) studied this question.