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. 1988 Dec 20;7(13):4129–4133. doi: 10.1002/j.1460-2075.1988.tb03307.x

Purification of brain D2 dopamine receptor.

R A Williamson 1, S Worrall 1, P L Chazot 1, P G Strange 1
PMCID: PMC455122  PMID: 3243275

Abstract

D2 dopamine receptors have been extracted from bovine brain using the detergent cholate and purified approximately 20,000-fold by affinity chromatography on haloperidol-sepharose and wheat germ agglutinin-agarose columns. The purified preparation contains D2 dopamine receptors as judged by the pharmacological specificity of [3H]spiperone binding to the purified material. The sp. act. of [3H]spiperone binding in the purified preparation is 2.5 nmol/mg protein. The purified preparation shows a major diffuse band at Mr 95,000 upon SDS-polyacrylamide gel electrophoresis and there is evidence for microheterogeneity either at the protein or glycosylation level. Photoaffinity labelling of D2 dopamine receptors also shows a species of Mr 95,000. The D2 dopamine receptor therefore is a glycoprotein of Mr 95,000.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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