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Specific purification of elongation factor 2 and isolation of its antibody

Authors :
Kiyoharu Takamatsu
Yoshio Okada
Tsuyoshi Uchida
Source :
Biochemical and Biophysical Research Communications. 134:1015-1021
Publication Year :
1986
Publisher :
Elsevier BV, 1986.

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 isoelectric 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.

Details

ISSN :
0006291X
Volume :
134
Database :
OpenAIRE
Journal :
Biochemical and Biophysical Research Communications
Accession number :
edsair.doi.dedup.....3074876efdd76b2db7c1921a188277aa
Full Text :
https://doi.org/10.1016/s0006-291x(86)80522-8