Elongation factor 2 (EF-2) was purified from rat liver extracts by affinity chromatography using fragment A of diphtheria toxin as the ligand. Purified EF-2 has a molecular weight of 96,000 and isolectric point of 6.6-6.8. The sequence of the nineteen N-terminal amino acid is Val-Asn-Phe-Thr-Val-Asp-Gln-Ile-Arg-Ala Ile-Met-Asp-Lys-Lys-Ala-Asn and the C-terminal amino acid is leucine. Purified rat EF-2 modified with ADP-ribose was injected into rabbits to prepare antibodies against EF-2. The anti-EF-2 antibodies can immunoprecipitate with EF-2 from various eukaryotic cells. © 1986 Academic Press, Inc. All rights reserved.
Takamatsu, K., Uchida, T., & Okada, Y. (1986). Specific purification of elongation factor 2 and isolation of its antibody. Biochemical and Biophysical Research Communications, 134(2), 1015–1021. https://doi.org/10.1016/S0006-291X(86)80522-8