Stabilization of the peripheral-type benzodiazepine acceptor by specific phospholipids.
The peripheral-type benzodiazepine acceptor from rat adrenal gland was solubilized with Triton X-100. The soluble acceptor exhibited isoquinoline carboxamide and benzodiazepine binding activity only when supplemented with lipid. Phosphatidylserine and phosphatidylinositol were especially efficacious. Such selectivity may reflect a specific structural requirement for acceptor activity. The requirement for lipid for acceptor activity in fractions subsequent to solubilization was demonstrated. This stabilization of acceptor activity by the phospholipids promises to facilitate purification of the functional acceptor.
Moynagh
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PN
Department of Biochemistry, Trinity College, University of Dublin, Ireland.
Williams
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D000311:Adrenal Glands / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D007546:Isoquinolines / Q000494:pharmacology; D008928:Mitochondria / Q000378:metabolism; D010716:Phosphatidylinositols / Q000494:pharmacology*; D010718:Phosphatidylserines / Q000494:pharmacology*; D011092:Polyethylene Glycols; D051381:Rats; D011963:Receptors, GABA-A / Q000187:drug effects / Q000302:isolation & purification*
D007546:Isoquinolines; D010716:Phosphatidylinositols; D010718:Phosphatidylserines; D011963:Receptors, GABA-A; D011092:Polyethylene Glycols; C037850:PK 11195