[3H]Mianserin binding to solubilized membranes of frontal cortex.
[3H]Mianserin binding sites were characterized in membranes of dog frontal cortex and solubilized with digitonin. The solubilized [3H]mianserin binding sites retained the binding characteristics of the membrane preparation. The dissociation constant (KD) for the soluble material was 2.2 nM which compared closely to that of the membrane-bound site (1.1 nM). Drug binding profiles indicated that the solubilized sites were both serotonergic and histaminergic in nature. Drugs active both H1- and S2-receptors potently displaced [3H]mianserin with Hill slopes close to 1. More selective serotonergic drugs such as LSD and spiperone competed for [3H]mianserin binding with shallow displacement curves. Of the neurotransmitters tested, serotonin was the most potent for both preparations. Because all the components of [3H]mianserin binding co-solubilize, the soluble material can be used to isolate individual sites.
D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D002540:Cerebral Cortex / Q000378:metabolism*; D003984:Dibenzazepines / Q000378:metabolism*; D004285:Dogs; D066298:In Vitro Techniques; D007700:Kinetics; D008566:Membranes / Q000378:metabolism; D008803:Mianserin / Q000378:metabolism*; D011092:Polyethylene Glycols; D013134:Spiperone / Q000378:metabolism; D013997:Time Factors
D003984:Dibenzazepines; D008803:Mianserin; D011092:Polyethylene Glycols; D013134:Spiperone