111 research outputs found
Illustrations du cours de microbiologie médicale :virologie
1re édition 1995-1996/1Syllabus strictement réservé aux étudiants suivant le cours de 2e candid. biologie médicale appliquée et 3e candid. médecineinfo:eu-repo/semantics/published
Génétique moléculaire :Illustrations
BIME3B, BIME3G, BIME3P, BIME3N, BIME3O, BIME3M - GENE005Ainfo:eu-repo/semantics/published
Applications médicales de l'ingénierie génétique
1re édition 1999-2000/1Syllabus strictement réservé aux étudiants suivant le cours de 1re Licence Sciences Biomédicales GENE 005info:eu-repo/semantics/published
Translation of mouse interferon mRNA in Xenopus laevis oocytes and in rabbit reticulocyte lysates
Mouse interferon mRNA, extracted from NDV (Newcastle disease virus)-induced L-929 cells has been translated with high efficiency in Xenopus laevis oocytes and rabbit reticulocyte lysates. The translational efficiency of a crude RNA extract was 10 640 interferon units/mg RNA/hour for the Xenopus oocytes and 4 012 interferon units/mg RNA/hour for the reticulocyte lysates. The translation product fulfilled the usual criteria for mouse interferon, viz. species specificity and neutralization by specific anti-mouse interferon antiserum. Upon injection of crude interferon mRNA into Xenopus oocytes, interferon activity appeared both in the oocyte homogenates and the oocyte incubation medium. When analyzed by velocity sedimentation in formamidesucrose, the mouse interferon mRNA showed a rather sharp peak halfway between the 4 S and 18 S RNA markers, as could be expected from a mRNA which codes for a 20,000 dalton protein. © 1978.SCOPUS: ar.jinfo:eu-repo/semantics/publishe
Mutagenesis of the human interleukin-6 fourth predicted alpha-helix: involvement of the Arg168 in the binding site.
Random substitutions of amino acid 161-184 of human interleukin-6 (hIL-6) have been generated at the cDNA level using oligonucleotide-directed mutagenesis. Among the majority of the mutant proteins showing a reduced biological activity on murine hybridoma cells, only those having a substitution of Met161, Arg168, Arg179 or Met184, retained a tertiary structure similar to the IL-6 folding. These residues are thus probably involved in the interaction with the IL-6 receptor. However, the contacts established by Arg168 and Arg179 seem far more important for the biological activity. According to Bazan's model of cytokine folding and the receptor binding site on the fourth alpha-helix, based on growth hormone similarity, we propose that Arg168 and Arg179 are located on the exposed surface of this presumed helix.Journal ArticleResearch Support, Non-U.S. Gov'tFLWNAinfo:eu-repo/semantics/publishe
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