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Reconstitution of affinity-purified dopamine D2...
Journal article

Reconstitution of affinity-purified dopamine D2 receptor binding activities by specific lipids

Abstract

The role of lipids in maintaining ligand binding properties of affinity-purified bovine striatal dopamine D2 receptor was investigated in detail. The receptor, purified on a haloperidol-linked Sepharose CL6B affinity column, exhibited low [3H]spiroperidol binding unless reconstituted with soybean phospholipids. In order to understand the role of individual phospholipids in maintaining the receptor binding activity, the purified preparation was …

Authors

Srivastava LK; Kazmi SMI; Blume AJ; Mishra RK

Journal

Biochimica et Biophysica Acta, Vol. 900, No. 2, pp. 175–182

Publisher

Elsevier

Publication Date

June 1987

DOI

10.1016/0005-2736(87)90331-2

ISSN

0006-3002