Purification of brain D2 dopamine receptor.
Purification of brain D2 dopamine receptor.
复制标题
脑 D2 多巴胺受体的纯化。
作者：
R. Williamson;S. Worrall;P. Chazot;P. Strange
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.
