Purification and characterization of the D sub(2)-dopamine receptor from bovine anterior pituitary

Purification and characterization of the D sub(2)-dopamine receptor from bovine anterior pituitary

The D sub(2)-dopamine receptor from bovine anterior pituitary has been purified similar to 33,000-fold to apparent homogeneity by sequential use of affinity chromatography on immobilized carboxymethylene-oximinospiperone-Sepharose, Datura stramonium) lectin-agarose, and hydroxylapatite chromatograph...

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Veröffentlicht in:The Journal of biological chemistry 1988-01, Vol.263 (35), p.18996-18002
Hauptverfasser: Senogles, SE, Amlaiky, N, Falardeau, P, Caron, M G
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dopamine D2
pituitary (anterior)
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container_end_page 18002
container_issue 35
container_start_page 18996
container_title The Journal of biological chemistry
container_volume 263
creator Senogles, SE
Amlaiky, N
Falardeau, P
Caron, M G
description The D sub(2)-dopamine receptor from bovine anterior pituitary has been purified similar to 33,000-fold to apparent homogeneity by sequential use of affinity chromatography on immobilized carboxymethylene-oximinospiperone-Sepharose, Datura stramonium) lectin-agarose, and hydroxylapatite chromatography. When reinserted into phospholipid vesicles with purified brain G sub(i)/G sub(o), the purified D sub(2) receptors mediate the agonist stimulation of super(35)S-labeled guanosine 5'-O-(thiotriphosphate) binding to brain G-proteins with a typical D sub(2)-dopaminergic order of potency. These data suggest that the authors have purified an intact functional D sub(2)-dopamine receptor.
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source EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection
subjects dopamine D2
pituitary (anterior)
title Purification and characterization of the D sub(2)-dopamine receptor from bovine anterior pituitary
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