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Journal of Receptor Research Volume 11, 1991 - Issue 6
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Research Article

Evaluation of 3H-CGP 12177 and 3H-DHA Binding to β2-Adrenoceptors of Rat Reticulocytes by Means of Affinity Spectra

Z. Kállay Institute of Preventive and Clinical Medicine, 833 01, Bratislava
,
J. Šmisterová Institute of Experimental Pharmacology, Slovak Academy of Sciences, 842 16, Bratislava, Czecho-Slovakia
,
L. Šoltés Institute of Experimental Pharmacology, Slovak Academy of Sciences, 842 16, Bratislava, Czecho-Slovakia
&
V. Marko Institute of Experimental Pharmacology, Slovak Academy of Sciences, 842 16, Bratislava, Czecho-Slovakia
Pages 909-917 | Published online: 26 Sep 2008
 
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Abstract

3H-CGP 12177 and 3H-DHA binding to rat reticulocyte β2-adrenoceptors by using an excess of 1×10−5 mol l−1 propranolol was evaluated by means of affinity spectra. To describe the 3H-CGP 12177 interaction with rat reticulocytes a binding isotherm valid for one single class of specific binding sites was found to be satisfactory. On the other hand, a more complex binding isotherm had to be used for the description of the 3H-DHA interaction with rat reticulocytes. This observation further supports the preferred application of 3H-CGP 12177 over 3H-DHA for radio-receptor assay of β-adrenoceptor blockers.

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