Literature DB >> 3511904

Specific purification of elongation factor 2 and isolation of its antibody.

K Takamatsu, T Uchida, Y Okada.   

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.

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Year:  1986        PMID： 3511904     DOI： 10.1016/s0006-291x(86)80522-8

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


  3 in total

1.  Amino acid sequence of mammalian elongation factor 2 deduced from the cDNA sequence: homology with GTP-binding proteins.

Authors:  K Kohno; T Uchida; H Ohkubo; S Nakanishi; T Nakanishi; T Fukui; E Ohtsuka; M Ikehara; Y Okada
Journal:  Proc Natl Acad Sci U S A       Date:  1986-07       Impact factor: 11.205

2.  Binding of monoclonal antibody specific for domain Ia/II of Pseudomonas aeruginosa exotoxin A at pH 4 strongly neutralizes exotoxin A-induced cytotoxicity in cell culture and in vivo.

Authors:  H Ohtsuka; K Horigome; A Higuchi; N Nomura; H Ochi; S Yokota; T Kohzuki; H Noguchi
Journal:  Infect Immun       Date:  1992-03       Impact factor: 3.609

3.  Application of fusogenic liposomes containing fragment A of diphtheria toxin to cancer therapy.

Authors:  H Mizuguchi; M Nakanishi; T Nakanishi; T Nakagawa; S Nakagawa; T Mayumi
Journal:  Br J Cancer       Date:  1996-02       Impact factor: 7.640
  3 in total

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