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  Purification and functional characterization of the human ß2-adrenergic receptor produced in baculovirus-infected insect cells

Reiländer, H., Boege, F., Vasudevan, S., Maul, G., Hekmann, M., Dees, C., et al. (1991). Purification and functional characterization of the human ß2-adrenergic receptor produced in baculovirus-infected insect cells. FEBS Letters, 282(2), 441-444. doi:10.1016/0014-5793(91)80532-8.

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 Urheber:
Reiländer, Helmut1, Autor           
Boege, Fritz2, Autor
Vasudevan, Subhash1, Autor           
Maul, Gabi1, Autor           
Hekmann, Mirko3, Autor
Dees, Christian3, Autor
Hampe, Wolfgang1, Autor
Helmreich, Ernst J.M.3, Autor
Michel, Hartmut1, Autor                 
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Medizinische Poliklinik der Universität Würzburg, Würtburg, Germany, ou_persistent22              
3Physiologisch-Chemisches Institut der Universität Würzburg, Würtburg, Germany, ou_persistent22              

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Schlagwörter: β-adrenergic receptor; Baculovirus; Expression; Glycosylation; Affinity chromatography; β2AR; β2-adrenergic receptor; CGP 12177; Ciba Geigy Product 12177; Con A; concanavalin A; Gs; stimulatory GTP binding protein; GTP[γ]S; guanosine 5′-O-(3-thiotriphosphate); [125I]ICYP; [125]iodocyanopindolol; [125I]ICYP-azided 2; [125I]iodocyanopindolol-azided 2; MOI; multiplicity of infection; SDS-PAGE; sodium dodecyl sulfate polyacrylamide gel electrophoresis; Sf9-cells; Spodoptera frugiperda cells; WGA; wheat germ agglutini
 Zusammenfassung: A human cDNA fragment bearing the complete coding region for the β2‐adrenergic receptor was introduced into the genome of Autographa california nuclear polyhedrosis virus under the control of the polyhedrin promoter. Binding studies using [125I]iodocynnopindolol showed that Sf9 insect cells infected with the recombinant virus expressed ≈ 1 × 104 β2‐adrenergic receptors on their cell surface. Photoaffinity labeling of whole cells and membraines revealed a molecular weight of ≈ 46000 for the expressed receptor. The receptor produced in insect cells is glycosylated but the extent and pattern differ from that of the receptor from human tissue. The heterologously expressed receptor was purified by alprenolol affinity chromatography, and was able to activate isolated Gs‐protein.

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Sprache(n): eng - English
 Datum: 1991-03-152001-12-141991-05-06
 Publikationsstatus: Erschienen
 Seiten: 4
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1016/0014-5793(91)80532-8
 Art des Abschluß: -

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Titel: FEBS Letters
  Andere : FEBS Lett.
Genre der Quelle: Zeitschrift
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Affiliations:
Ort, Verlag, Ausgabe: Amsterdam : Elsevier
Seiten: - Band / Heft: 282 (2) Artikelnummer: - Start- / Endseite: 441 - 444 Identifikator: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501