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Purification of bovine striatal dopamine D-2...
Journal article

Purification of bovine striatal dopamine D-2 receptor by affinity chromatography.

Abstract

Bovine striatal dopamine D-2 receptor has been purified approximately 2000-fold by affinity chromatography. The receptor, solubilized with cholic acid and sodium chloride, was adsorbed on haloperidol-linked Sepharose CL-6B and eluted with spiroperidol. The adsorption of receptor to the affinity matrix was biospecific as preincubation of the solubilized preparation with D-2 receptor agonists or antagonists blocked retention of receptor. The …

Authors

Ramwani J; Mishra RK

Journal

Journal of Biological Chemistry, Vol. 261, No. 19, pp. 8894–8898

Publisher

Elsevier

Publication Date

7 1986

DOI

10.1016/s0021-9258(19)84466-6

ISSN

0021-9258