A study of the kinetics of the interaction of spiperone with binding sites on human mononuclear cells: existence of a heterogeneous population of spiperone binding sites.
The kinetics and equilibrium of the interaction of [3H]spiperone with binding sites on human mononuclear cells were studied using a competitive displacement of spiperone by ketanserin, sulpiride, haloperidol, (+)- and (-)-butaclamol. [3H]Spiperone binding sites on human mononuclear cells were shown to be not of the D2, but most probably of the 5-HT2 type. The process of [3H]spiperone binding to these sites conforms to the model of ligand interaction with two independent binding sites (the high-affinity site, Kd1 = 3 nM and the low-affinity site, Kd2 = 20 nM), thus suggesting heterogeneity of spiperone sites on mononuclear cells. We found that in contrast to high-affinity binding sites, low-affinity sites show an essentially lower stability during storage of mononuclear cells.
Zaitsev
S V
SV
A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, M.V. Lomonosov Moscow State University, USSR.
Koshkin
A A
AA
Izumrudova
I I
II
Varfolomeev
S D
SD
D001665:Binding Sites; D002478:Cells, Cultured; D006801:Humans; D007700:Kinetics; D007963:Leukocytes, Mononuclear / Q000378:metabolism*; D011985:Receptors, Serotonin / Q000378:metabolism; D013134:Spiperone / Q000378:metabolism*
D011985:Receptors, Serotonin; D013134:Spiperone