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Title: | Solubilization and characterization of endothelin-1 receptors in rat cardiac tissue. | Austin Authors: | Liu, J J;Kelly, J;Casley, David J;Johnston, Colin I;Nayler, W G | Affiliation: | Department of Medicine, University of Melbourne, Austin Hospital, Heidelberg, Victoria, Australia | Issue Date: | 15-Jan-1990 | Publication information: | Biochemical and Biophysical Research Communications; 166(1): 299-307 | Abstract: | Adult rat cardiac endothelin-1 (ET-1) receptors were solubilized with 0.5% digitonin and then characterized. The receptors retained binding activity after solubilization. Binding was saturable (KD of 0.065 +/- 0.004 nM, Bmax of 94.6 +/- 4.5 fmol/mg protein; Hill coefficient of 0.987 +/- 0.017 n = 6) and pH dependent, with the binding increasing as the pH was decreased from 10 to 4, but decreasing dramatically as pH dropped to 2. Specifically bound [125I]-ET-1 was not dissociated by 2 x 10(-7) M unlabelled ET-1, but was dissociated by pH 10 and 2. Returning the pH to 7.4 restored the binding activity of the receptors. Unlabelled ET-1 (10(-12) - 10(-7) M) and sarafotoxin S6b(10(-12) - 10(-7) M) competed with [125I]-ET-1 for binding to the receptors. | Gov't Doc #: | 2154201 | URI: | http://ahro.austin.org.au/austinjspui/handle/1/11254 | Journal: | Biochemical and biophysical research communications | URL: | https://pubmed.ncbi.nlm.nih.gov/2154201 | Type: | Journal Article | Subjects: | Animals Binding, Competitive Cell Membrane.metabolism Digitonin Endothelins Endothelium, Vascular Female Hydrogen-Ion Concentration Kinetics Myocardium.metabolism Peptides.metabolism Rats Rats, Inbred Strains Receptors, Cell Surface.isolation & purification.metabolism Receptors, Endothelin |
Appears in Collections: | Journal articles |
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