Purification and functional characterization of the human beta 2-adrenergic receptor produced in baculovirus-infected insect cells.
Standard
Purification and functional characterization of the human beta 2-adrenergic receptor produced in baculovirus-infected insect cells. / Reiländer, H; Boege, F; Vasudevan, S; Maul, G; Hekman, M; Dees, C; Hampe, Wolfgang; Helmreich, E J; Michel, H.
in: FEBS LETT, Jahrgang 282, Nr. 2, 2, 1991, S. 441-444.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
Harvard
APA
Vancouver
Bibtex
}
RIS
TY - JOUR
T1 - Purification and functional characterization of the human beta 2-adrenergic receptor produced in baculovirus-infected insect cells.
AU - Reiländer, H
AU - Boege, F
AU - Vasudevan, S
AU - Maul, G
AU - Hekman, M
AU - Dees, C
AU - Hampe, Wolfgang
AU - Helmreich, E J
AU - Michel, H
PY - 1991
Y1 - 1991
N2 - A human cDNA fragment bearing the complete coding region for the beta 2-adrenergic receptor was introduced into the genome of Autographa california nuclear polyhedrosis virus under the control of the polyhedrin promoter. Binding studies using [125I]iodocyanopindolol showed that Sf9 insect cells infected with the recombinant virus expressed approximately 1 x 10(6) beta 2-adrenergic receptors on their cell surface. Photoaffinity labeling of whole cells and membranes revealed a molecular weight of approximately 46,000 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.
AB - A human cDNA fragment bearing the complete coding region for the beta 2-adrenergic receptor was introduced into the genome of Autographa california nuclear polyhedrosis virus under the control of the polyhedrin promoter. Binding studies using [125I]iodocyanopindolol showed that Sf9 insect cells infected with the recombinant virus expressed approximately 1 x 10(6) beta 2-adrenergic receptors on their cell surface. Photoaffinity labeling of whole cells and membranes revealed a molecular weight of approximately 46,000 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.
M3 - SCORING: Zeitschriftenaufsatz
VL - 282
SP - 441
EP - 444
JO - FEBS LETT
JF - FEBS LETT
SN - 0014-5793
IS - 2
M1 - 2
ER -