Reconstitution of a purified mu-opioid binding protein in liposomes: selective, high affinity, GTP gamma S-sensitive mu-opioid agonist binding is restored
| Autor: | Li-Qun Fan, Y H Yao, Jacob M. Hiller, D. Ofri, T. L. Gioannini, Eric J. Simon, L. Hyde |
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| Rok vydání: | 1993 |
| Předmět: |
Narcotics
G protein Biophysics Synthetic membrane Receptors Opioid mu Biology Biochemistry Binding Competitive Chaps Animals Binding site Opioid peptide Molecular Biology Liposome Binding Sites Morphine Naloxone Binding protein Cell Membrane Cholic Acids Cell Biology Enkephalins Enkephalin Ala(2)-MePhe(4)-Gly(5) Corpus Striatum Kinetics Guanosine 5'-O-(3-Thiotriphosphate) Second messenger system Liposomes Cattle Enkephalin D-Penicillamine (2 5) |
| Zdroj: | Biochemical and biophysical research communications. 194(2) |
| ISSN: | 0006-291X |
| Popis: | An opioid binding protein (OBP) purified to homogeneity from bovine striatal membranes has been reconstituted in liposomes. The liposomes were produced by PEG-precipitation of OBP in the presence of a CHAPS extract of bovine striatum, devoid of opioid binding. High affinity μ-agonist binding was restored. The binding was selective for μ-agonists, stereospecific and inhibited by GTPγS. These results demonstrate that there is recoupling of OBP with G-protein and confirm our earlier evidence that the purified OBP is a μ-opioid binding site. |
| Databáze: | OpenAIRE |
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