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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||URL:||https://pubmed.ncbi.nlm.nih.gov/2154201||Type:||Journal Article||Subjects:||Animals
Rats, Inbred Strains
Receptors, Cell Surface.isolation & purification.metabolism
|Appears in Collections:||Journal articles|
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