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. 1972 May;69(5):1327–1331. doi: 10.1073/pnas.69.5.1327

Spatial Arrangement of Ribosomal Proteins: Reaction of the Escherichia coli 30S Subunit with bis-Imidoesters

T A Bickle 1, J W B Hershey 1, R R Traut 1
PMCID: PMC426692  PMID: 4556460

Abstract

The 30S ribosomal subunit of E. coli was treated with the bifunctional reagent bis-(methyl)suberimidate. Crosslinked ribosomal proteins were identified as bands with increased molecular weight after electrophoresis in polyacrylamide gels containing sodium dodecyl sulphate. The pattern of crosslinked products was altered when unfolded subunits were used. Free ribosomal protein was not crosslinked. Several of the crosslinked products were cleaved by ammonolysis to form the original monomeric protein constituents. The low yields of the reactions necessitated the use of radioactive proteins and auto-radiographic procedures. The crosslinked proteins were tentatively identified by coelectrophoresis of the radioactive ammonolysis products with carrier 30S protein in sodium dodecyl sulphate, and coelectrophoresis at pH 4.5 in buffers containing urea.

Keywords: gel electrophoresis, crosslinking reagent, bis-(methyl)suberimidate

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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