The high-affinity binding site for [3H]Ro 5-4864 has been solubilized from rat kidney using 1% Triton X-100. After lowering the concentration of detergent and using a poly(ethylene glycol) gamma-globulin assay, it has been possible to demonstrate solubilization of about 90% of the binding sites. A single soluble class of binding sites with a Kd of 1.8 nM is found. The order of potency of benzodiazepines is identical for the solubilized receptor and the membrane-bound form. Gel filtration revealed a major peak of binding activity with apparent molecular weight of 215000 and a Stokes' radius of 5.03 nm.
SOLUBILIZATION OF RAT-KIDNEY BENZODIAZEPINE BINDING-SITES
MARTINI, CLAUDIA;GIANNACCINI, GINO;LUCACCHINI, ANTONIO
1983-01-01
Abstract
The high-affinity binding site for [3H]Ro 5-4864 has been solubilized from rat kidney using 1% Triton X-100. After lowering the concentration of detergent and using a poly(ethylene glycol) gamma-globulin assay, it has been possible to demonstrate solubilization of about 90% of the binding sites. A single soluble class of binding sites with a Kd of 1.8 nM is found. The order of potency of benzodiazepines is identical for the solubilized receptor and the membrane-bound form. Gel filtration revealed a major peak of binding activity with apparent molecular weight of 215000 and a Stokes' radius of 5.03 nm.File in questo prodotto:
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