Production of an antiserum specific to the ADP-ribosylated form of elongation factor 2 from archaebacteria and eukaryotes.
An antiserum to ADP-ribosylated elongation factor 2 (ADPR- EF-2) from S. acidocaldarius was raised in rabbits using stained, homogenized, ADPR- EF-2-containing slices from SDS-gels as a source of antigen. Elongation factor 2 ( EF-2) from S. acidocaldarius was cloned in E. coli and the expressed gene product was used in order to adsorb all anti- EF-2 antibodies which do not contain the ADP-ribosyl group within their epitopes, as E. coli is unable to synthesize the ADP-ribosyl acceptor diphthamide. The remaining antibodies were specific to ADP-ribosylated EF-2 from Thermoplasma acidophilum, S. acidocaldarius and Desulfurococcus mucosus. ADP-ribosylated EF-2 from eukaryotic sources also reacted with the adsorbed antiserum as shown for EF-2 isolated from the killi-fish Cynolebias whitei, the mouse species BALB/c and Han/Wistar rats. The adsorbed antiserum did not cross-react with ADP-ribosylated actin or rho protein or with FAD-containing D-amino acid oxidase.[1]References
- Production of an antiserum specific to the ADP-ribosylated form of elongation factor 2 from archaebacteria and eukaryotes. Siegmund, K.D., Klink, F. FEBS Lett. (1992) [Pubmed]
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