Specific purification of elongation factor 2 and isolation of its antibody

  • Takamatsu K
  • Uchida T
  • Okada Y
  • 5

    Readers

    Mendeley users who have this article in their library.
  • 6

    Citations

    Citations of this article.

Abstract

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.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Authors

  • Kiyoharu Takamatsu

  • Tsuyoshi Uchida

  • Yoshio Okada

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free