[3H]Spiroperidol binding in rat striatum: two high-affinity sites of differing selectivities.

Abstract:

:[3H]Spiroperidol binding to homogenates of rat striatum is saturable and shows either monophasic or biphasic saturation isotherms under specified conditions. In poorly washed membrane fragment preparations, saturation isotherms of [3H]spiroperidol binding are monophasic, revealing an apparently homogeneous set of sites with KD 0.6 +/- 0.3 nM and density 440 +/- 80 fmol/mg protein. However, equilibrium displacement studies of [3H]spiroperidol binding at this site indicate an alpha-adrenergic component in addition to the previously described dopaminergic component. In thoroughly washed membrane fragment preparations, saturation isotherms are clearly biphasic, showing an additional high-affinity site with an approximate KD of 24 +/- 10 pM and an approximate density of 110 +/- 20 fmol/mg protein at a protein concentration of 2.0 mg/ml. Selectivity at this site appears classically dopaminergic, suggesting that the lower affinity site is the primary source of the alpha-adrenergic component of spiroperidol binding.

journal_name

J Neurochem

authors

Andorn AC,Maguire ME

doi

10.1111/j.1471-4159.1980.tb07865.x

subject

Has Abstract

pub_date

1980-11-01 00:00:00

pages

1105-13

issue

5

eissn

0022-3042

issn

1471-4159

journal_volume

35

pub_type

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