FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2012324795> ?p ?o ?g. }

• W2012324795 abstract "The role of lipids in maintaining ligand binding properties of affinity-purified bovine striatal dopamine D2 receptor was investigated in detail. The receptor, purified on a haloperidol-linked Sepharose CL6B affinity column, exhibited low [3H]spiroperidol binding unless reconstituted with soybean phospholipids. In order to understand the role of individual phospholipids in maintaining the receptor binding activity, the purified preparation was reconstituted separately with individual phospholipids and assayed for [3H]spiroperidol binding. Except for phosphatidylcholine and phosphatidylethanolamine, that respectively restored 30 and 20% binding as compared to that obtained with soybean lipids, reconstitution with other lipids had very little effect. When various combinations of phospholipids were used for reconstitution, a phosphatidylcholine and phosphatidylserine mixture seemed to almost fully restore the receptor binding. A mixture of phosphatidylcholine and phosphatidylethanolamine was as effective as phosphatidylcholine alone in reconstituting ligand binding; however, when phosphatidylserine was also included in the mixture, there was a pronounced increase in binding (about 2-fold compared to the soybean lipids and about 6-fold compared to the phosphatidylcholine-phosphatidylethanolamine mixture). Substitution of other phospholipids or cholesterol for phosphatidylserine in phosphatidylcholine and phosphatidylethanolamine mixture had little effect. Maximal reconstitution of [3H]spiroperidol binding was obtained with phosphatidylcholine, phosphatidylethanolamine and phosphatidylserine mixture (2:2:1, w/w) at a concentration of 0.5 mg/ml. The reconstituted receptor exhibited high affinity binding for [3H]spiroperidol which was comparable to that obtained with membrane or solubilized preparations. Various dopaminergic antagonists and agonists showed appropriate order of potency for the reconstituted receptor. The presently described reconstitution data suggest a role of specific phospholipids in preserving the binding properties of dopamine D2 receptor and should prove useful in studies on functional reconstitution of the receptor." @default.
• W2012324795 created "2016-06-24" @default.
• W2012324795 creator A5002413814 @default.
• W2012324795 creator A5014184827 @default.
• W2012324795 creator A5052979149 @default.
• W2012324795 creator A5076596007 @default.
• W2012324795 date "1987-06-01" @default.
• W2012324795 modified "2023-09-27" @default.
• W2012324795 title "Reconstitution of affinity-purified dopamine D2 receptor binding activities by specific lipids" @default.
• W2012324795 cites W1479951874 @default.
• W2012324795 cites W1548557192 @default.
• W2012324795 cites W1560215073 @default.
• W2012324795 cites W1964490459 @default.
• W2012324795 cites W1981089905 @default.
• W2012324795 cites W1986215971 @default.
• W2012324795 cites W1994837128 @default.
• W2012324795 cites W2030481280 @default.
• W2012324795 cites W2036626711 @default.
• W2012324795 cites W2053386876 @default.
• W2012324795 cites W2066954853 @default.
• W2012324795 cites W2074785483 @default.
• W2012324795 cites W2082497364 @default.
• W2012324795 cites W2092994032 @default.
• W2012324795 cites W2095078357 @default.
• W2012324795 cites W2125505240 @default.
• W2012324795 cites W2132376958 @default.
• W2012324795 cites W2329224281 @default.
• W2012324795 cites W237311064 @default.
• W2012324795 doi "https://doi.org/10.1016/0005-2736(87)90331-2" @default.
• W2012324795 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2954584" @default.
• W2012324795 hasPublicationYear "1987" @default.
• W2012324795 type Work @default.
• W2012324795 sameAs 2012324795 @default.
• W2012324795 citedByCount "14" @default.
• W2012324795 crossrefType "journal-article" @default.
• W2012324795 hasAuthorship W2012324795A5002413814 @default.
• W2012324795 hasAuthorship W2012324795A5014184827 @default.
• W2012324795 hasAuthorship W2012324795A5052979149 @default.
• W2012324795 hasAuthorship W2012324795A5076596007 @default.
• W2012324795 hasConcept C170493617 @default.
• W2012324795 hasConcept C185592680 @default.
• W2012324795 hasConcept C2776330855 @default.
• W2012324795 hasConcept C2778918659 @default.
• W2012324795 hasConcept C2779637612 @default.
• W2012324795 hasConcept C2781170229 @default.
• W2012324795 hasConcept C41625074 @default.
• W2012324795 hasConcept C55493867 @default.
• W2012324795 hasConceptScore W2012324795C170493617 @default.
• W2012324795 hasConceptScore W2012324795C185592680 @default.
• W2012324795 hasConceptScore W2012324795C2776330855 @default.
• W2012324795 hasConceptScore W2012324795C2778918659 @default.
• W2012324795 hasConceptScore W2012324795C2779637612 @default.
• W2012324795 hasConceptScore W2012324795C2781170229 @default.
• W2012324795 hasConceptScore W2012324795C41625074 @default.
• W2012324795 hasConceptScore W2012324795C55493867 @default.
• W2012324795 hasLocation W20123247951 @default.
• W2012324795 hasLocation W20123247952 @default.
• W2012324795 hasOpenAccess W2012324795 @default.
• W2012324795 hasPrimaryLocation W20123247951 @default.
• W2012324795 hasRelatedWork W1520073414 @default.
• W2012324795 hasRelatedWork W1522769801 @default.
• W2012324795 hasRelatedWork W1970327695 @default.
• W2012324795 hasRelatedWork W1980929094 @default.
• W2012324795 hasRelatedWork W2016583698 @default.
• W2012324795 hasRelatedWork W2048465125 @default.
• W2012324795 hasRelatedWork W2068725935 @default.
• W2012324795 hasRelatedWork W2071203160 @default.
• W2012324795 hasRelatedWork W2317954243 @default.
• W2012324795 hasRelatedWork W950194781 @default.
• W2012324795 isParatext "false" @default.
• W2012324795 isRetracted "false" @default.
• W2012324795 magId "2012324795" @default.
• W2012324795 workType "article" @default.