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Marullo, S., Laboratoire de Biologie Moleculaire des Recepteurs, Centre National de la Recherche Scientifique, Universite Paris VII, 75724 Paris Cedex 15, France
Delavier-Klutchko, C., Laboratoire de Biologie Moleculaire des Recepteurs, Centre National de la Recherche Scientifique, Universite Paris VII, 75724 Paris Cedex 15, France
Eshdat, Y., Laboratoire de Biologie Moleculaire des Recepteurs, Centre National de la Recherche Scientifique, Universite Paris VII, 75724 Paris Cedex 15, France
Strosberg, A.D., Laboratoire de Biologie Moleculaire des Recepteurs, Centre National de la Recherche Scientifique, Universite Paris VII, 75724 Paris Cedex 15, France
Emorine, L., Laboratoire de Biologie Moleculaire des Recepteurs, Centre National de la Recherche Scientifique, Universite Paris VII, 75724 Paris Cedex 15, France
The coding region of the gene for the human β2-adrenergic receptor gene was fused to the β-galactosidase gene of the λgt11 expression vector. The Y1089 Escherichia coli strain was lysogenized with this modified vector and transcription of the fusion gene was induced. Expression of this transcription unit was shown by the appearance in the bacteria of proteins of molecular weight higher than that of native β-galactosidase, which are immunoreactive with anti-β-galactosidase antibodies. Production of β2-adrenergic receptors was shown by the presence, on intact bacteria, of binding sites for catecholamine agonists and antagonists possessing a typical β2-adrenergic pharmacological profile. Binding and photoaffinity labeling studies performed on intact E. coli and its membrane fractions showed that these binding sites are located in the inner membrane of the bacteria. Expression of pharmacologically active human β2-adrenergic receptors in E. coli further supports the similar transmembrane organization proposed for bacteriorhodopsin and eukaryotic membrane-embedded receptors coupled to guanine nucleotide-binding regulatory proteins. Moreover, this system should facilitate future analyses of the ligand-binding properties within this family of membrane receptors.
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תנאי שימוש
Human β2-adrenergic receptors expressed in Escherichia coli membranes retain their pharmacological properties
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Marullo, S., Laboratoire de Biologie Moleculaire des Recepteurs, Centre National de la Recherche Scientifique, Universite Paris VII, 75724 Paris Cedex 15, France
Delavier-Klutchko, C., Laboratoire de Biologie Moleculaire des Recepteurs, Centre National de la Recherche Scientifique, Universite Paris VII, 75724 Paris Cedex 15, France
Eshdat, Y., Laboratoire de Biologie Moleculaire des Recepteurs, Centre National de la Recherche Scientifique, Universite Paris VII, 75724 Paris Cedex 15, France
Strosberg, A.D., Laboratoire de Biologie Moleculaire des Recepteurs, Centre National de la Recherche Scientifique, Universite Paris VII, 75724 Paris Cedex 15, France
Emorine, L., Laboratoire de Biologie Moleculaire des Recepteurs, Centre National de la Recherche Scientifique, Universite Paris VII, 75724 Paris Cedex 15, France
Human β2-adrenergic receptors expressed in Escherichia coli membranes retain their pharmacological properties
The coding region of the gene for the human β2-adrenergic receptor gene was fused to the β-galactosidase gene of the λgt11 expression vector. The Y1089 Escherichia coli strain was lysogenized with this modified vector and transcription of the fusion gene was induced. Expression of this transcription unit was shown by the appearance in the bacteria of proteins of molecular weight higher than that of native β-galactosidase, which are immunoreactive with anti-β-galactosidase antibodies. Production of β2-adrenergic receptors was shown by the presence, on intact bacteria, of binding sites for catecholamine agonists and antagonists possessing a typical β2-adrenergic pharmacological profile. Binding and photoaffinity labeling studies performed on intact E. coli and its membrane fractions showed that these binding sites are located in the inner membrane of the bacteria. Expression of pharmacologically active human β2-adrenergic receptors in E. coli further supports the similar transmembrane organization proposed for bacteriorhodopsin and eukaryotic membrane-embedded receptors coupled to guanine nucleotide-binding regulatory proteins. Moreover, this system should facilitate future analyses of the ligand-binding properties within this family of membrane receptors.
Scientific Publication
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