Soluble spiroperidol binding factors from bovine caudate nucleus.
Several properties of soluble spiroperidol binding factors separated from bovine caudate nucleus have been investigated by a previously unreported procedure. Data consistent with high particle weight and rapid binding equilibration are reported for high-affinity (+)butaclamol-sensitive components of a digitonin extract. A slower sedimenting component is found that also exhibits high affinity for spiroperidol but is not sensitive to (+)butaclamol. Centrifugation of a caudate nucleus homogenate yields a supernatant that appears to contain a component that exhibits spiroperidol binding that is more sensitive to displacement by (-) than by (+)butaclamol. The procedure used effects rapid separation of bound from unbound tritiated ligand on short columns of Sephadex G-15 followed by extrusion and sectioning of the Sephadex. The radioactivity remaining with each section is determined. The procedure is very rapid; the addition of active phases or the changing of the ionic environment, which may disturb the equilibrium, is avoided; and recovery of the protein free of bound ligand is easily affected.
D000818:Animals; D001665:Binding Sites; D002069:Butaclamol / Q000494:pharmacology; D002090:Butyrophenones / Q000378:metabolism*; D002417:Cattle; D002421:Caudate Nucleus / Q000378:metabolism*; D007700:Kinetics; D013134:Spiperone / Q000378:metabolism*; D013347:Subcellular Fractions / Q000378:metabolism
D002090:Butyrophenones; D013134:Spiperone; D002069:Butaclamol