| Literature DB >> 775317 |
T Girbes, D Vazquez, J Modolell.
Abstract
Treatment of elongation factor G (EF-G) with the thiol reagent N-ethylmaleimide only partially inhibits (10 to 70%) the activity of the factor in (a) guanosine nucleotide-EF-G-ribosome complex formation, (b) uncoupled ribosome-dependent GTP hydrolysis, and (c) polypeptide synthesis. Moreover, a similar treatment of the factor with N-[3H]ethylmaleimide does not lead to 3H-label being associated with a GDP-EF-G-ribosome-fusidic acid complex. Thus, the results indicate the presence in EF-G preparations of a form of the factor that does not react with N-ethylmaleimide.Entities:
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Year: 1976 PMID： 775317 DOI： 10.1007/bf00366262
Source DB: PubMed Journal: Mol Biol Rep ISSN： 0301-4851 Impact factor: 2.316