Chazot, J.A., Strange, Philip G. (1992) COUPLING OF D2-DOPAMINE RECEPTORS TO G-PROTEINS IN SOLUBILIZED PREPARATIONS OF BOVINE CAUDATE-NUCLEUS. Biochemical Journal, 281 . pp. 369-375. ISSN 0264-6021. (doi:10.1042/bj2810369) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:23255)
| The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. | |
| Official URL: https://doi.org/10.1042/bj2810369 |
|
Abstract
1. The coupling of D2 dopamine receptors and G-proteins has been examined in cholate-solubilized preparations of bovine caudate nucleus. 2. No receptor-G-protein coupling could be detected in solubilized preparations obtained in 0.3% cholate, but if this preparation is diluted 5-fold, coupling is re-established. 3. The dilution process was examined, and it was shown that the change in ionic strength was an important factor in modulating the observed receptor-G-protein interaction. 4. Ionic strength was shown, however, not to be the primary determinant of receptor-G-protein coupling. This is likely to be the formation, upon dilution of the preparation, of vesicles in which receptor and G-protein reassociate. 5. The formation of vesicles upon dilution was examined by a variety of techniques, including thermal-stability studies, gel filtration, centrifugation and clectron microscopy.
| Item Type: | Article |
|---|---|
| DOI/Identification number: | 10.1042/bj2810369 |
| Subjects: |
Q Science > QP Physiology (Living systems) > QP517 Biochemistry Q Science > QP Physiology (Living systems) > QP506 Molecular biology |
| Institutional Unit: | Schools > School of Natural Sciences > Biosciences |
| Former Institutional Unit: |
Divisions > Division of Natural Sciences > Biosciences
|
| Depositing User: | A. Xie |
| Date Deposited: | 01 Nov 2009 20:08 UTC |
| Last Modified: | 20 May 2025 09:16 UTC |
| Resource URI: | https://kar.kent.ac.uk/id/eprint/23255 (The current URI for this page, for reference purposes) |
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