Dopamine D2 receptors, detected by [3H]spiperone Dopamine D2 receptors, detected by [3H]spiperone binding, were solubilized from bovine caudate nucleus by cholate/sodium chloride and were found to bind to wheat germ agglutinin immobilized on agarose. Specific elution could be achieved with N-acetylglucosamine whereas other sugars tested were inactive in this regard. The eluted preparation was enriched in solubilized receptors about sevenfold. The pharmaco-logical properties of the preparation were essentially unchanged by the lectin affinity purification procedure. The D2 dopamine receptor is therefore a glycoprotein. binding, were solubilized from bovine caudate nucJeus by cholate/sodium chloride and were found to bind to wheat germ agglutinin immobilized on agarose. Specific elution could be achieved with N-acetylglucosamine whereas other sugars tested were inactive in this regard. The eluted preparation was enriched in solubilized receptors about sevenfold. The pharmacological properties of the preparation were essentially unchanged by the lectin affinity purification procedure. The D2 dopamine receptor is therefore a glycoprotein.
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Research Article|
April 01 1985
Partial purification of dopamine D2 receptors using lectin affinity columns
W. Mark Abbott;
W. Mark Abbott
1Department of Biochemistry, The Medical School, Queen's Medical Centre, Nottingham NG7 2UH, UK
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Philip G. Strange
Philip G. Strange
1Department of Biochemistry, The Medical School, Queen's Medical Centre, Nottingham NG7 2UH, UK
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Publisher: Portland Press Ltd
Received:
March 28 1985
Online ISSN: 1573-4935
Print ISSN: 0144-8463
© 1985 The Biochemical Society
1985
Biosci Rep (1985) 5 (4): 303–308.
Article history
Received:
March 28 1985
Citation
W. Mark Abbott, Philip G. Strange; Partial purification of dopamine D2 receptors using lectin affinity columns. Biosci Rep 1 April 1985; 5 (4): 303–308. doi: https://doi.org/10.1007/BF01116901
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