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Specific purification of elongation factor 2 and isolation of its antibody
- 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.
- Subjects :
- Immunoprecipitation
Biophysics
Saccharomyces cerevisiae
Cross Reactions
Biology
Biochemistry
Antibodies
Chromatography, Affinity
Mice
Peptide Elongation Factor 2
Affinity chromatography
Antibody Specificity
Animals
Diphtheria Toxin
Amino Acid Sequence
Isoelectric Point
Molecular Biology
Diphtheria toxin
chemistry.chemical_classification
Cell Biology
Peptide Elongation Factors
Ligand (biochemistry)
Molecular biology
Rats
Amino acid
Molecular Weight
Elongation factor
Liver
chemistry
biology.protein
Leucine
Antibody
Subjects
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