Please use this identifier to cite or link to this item: http://ahro.austin.org.au/austinjspui/handle/1/11254
Title: Solubilization and characterization of endothelin-1 receptors in rat cardiac tissue.
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
Citation: 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.
Internal ID Number: 2154201
URI: http://ahro.austin.org.au/austinjspui/handle/1/11254
URL: http://www.ncbi.nlm.nih.gov/pubmed/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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