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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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 Creators:
Reiländer, Helmut1, Author           
Boege, Fritz2, Author
Vasudevan, Subhash1, Author           
Maul, Gabi1, Author           
Hekmann, Mirko3, Author
Dees, Christian3, Author
Hampe, Wolfgang1, Author
Helmreich, Ernst J.M.3, Author
Michel, Hartmut1, Author                 
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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Free keywords: 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
 Abstract: 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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Language(s): eng - English
 Dates: 1991-03-152001-12-141991-05-06
 Publication Status: Issued
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/0014-5793(91)80532-8
 Degree: -

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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
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Affiliations:
Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 282 (2) Sequence Number: - Start / End Page: 441 - 444 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501