Binding of 125 I-Cyanopindolol to Beta-1-Adreno-Ceptors in a High and Low Affinity State
- 1 January 1983
- journal article
- research article
- Published by Taylor & Francis in Journal of Receptor Research
- Vol. 3 (1-2) , 45-59
- https://doi.org/10.3109/10799898309041922
Abstract
Investigation of binding properties of (+), (−) and (±)125Iodocyanopindolol (ICYP) to ß1-adrenoceptors of guinea pig left ventricle membranes revealed that these radioligands bind to receptors in a high and low affinity state which is not influenced by guanylnucleotides. The contribution of the (+)enantiomer to the binding of the racemic ligand at low receptor concentrations can be neglected since the dissociation time courses of (±) and (−)ICYP are identical. The existence of two affinity states of ß-adrenoceptors interacting with the antagonist ICYP was evident from 1: biphasic dissociation kinetics and 2: from curvilinear Scatchard plots.Keywords
This publication has 5 references indexed in Scilit:
- (±)[125Iodo]cyanopindolol, a new ligand for β-adrenoceptors: Identification and quantitation of subclasses of β-adrenoceptors in guinea pigNaunyn-Schmiedebergs Archiv für experimentelle Pathologie und Pharmakologie, 1981
- ?-Adrenoceptor blocking agents as partial agonists in isolated heart muscle: Dissociation of stimulation and blockadeNaunyn-Schmiedebergs Archiv für experimentelle Pathologie und Pharmakologie, 1980
- Activation of heart sarcolemmal Ca2+Mg2+ ATPase by cyclic AMP-dependent protein kinaseBiochemical and Biophysical Research Communications, 1979
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- β-Adrenergic Receptor: Stereospecific Interaction of Iodinated β-Blocking Agent with High Affinity SiteScience, 1974