title: Involvement of GTP-regulatory protein in brain prostaglandin E2 receptor and separation of the two components.
abstract: The specific binding protein for prostaglandin (PG) E2 solubilized from porcine brain was sensitive to guanine nucleotides. GTP inhibited the association and enhanced the dissociation of the specific [3H]PGE2 binding. Scatchard analyses showed that GTP (10 microM) decreased the binding affinity more than 3-fold without major change in the number of binding site. Gel filtration separated the binding site from GTP-regulatory component (N). The separated binding protein had a reduced affinity to PGE2 and lost its sensitivity to GTP. The addition of the separated N restored its responsiveness to GTP, and also increased the binding affinity to the original level. These results provide direct evidence for the molecular interaction between the PGE2 binding protein and N in the brain.
authors.forename: N
authors.initials: N
authors.lastname: Yumoto
authors.forename: M
authors.initials: M
authors.lastname: Hatanaka
authors.forename: Y
authors.initials: Y
authors.lastname: Watanabe
authors.forename: O
authors.initials: O
authors.lastname: Hayaishi
mesh_terms: D000818:Animals; D001921:Brain / Q000378:metabolism*; D002793:Cholic Acids; D019204:GTP-Binding Proteins / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000494:pharmacology; D007700:Kinetics; D046911:Macromolecular Substances; D011485:Protein Binding / Q000187:drug effects; D011956:Receptors, Cell Surface / Q000378:metabolism*; D011982:Receptors, Prostaglandin / Q000302:isolation & purification / Q000378:metabolism*; D018078:Receptors, Prostaglandin E; D013552:Swine
chemical_list: D002793:Cholic Acids; D046911:Macromolecular Substances; D011956:Receptors, Cell Surface; D011982:Receptors, Prostaglandin; D018078:Receptors, Prostaglandin E; D006160:Guanosine Triphosphate; D019204:GTP-Binding Proteins; C028213:3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate