Please use this identifier to cite or link to this item: http://ahro.austin.org.au/austinjspui/handle/1/12562
Title: Specific high-affinity binding sites for 125I-labelled porcine endothelin in rat cardiac membranes.
Authors: Gu, X H;Casley, David J;Nayler, W
Affiliation: Department of Medicine, University of Melbourne, Austin Hospital, Heidelberg, Victoria, Australia.
Issue Date: 22-Aug-1989
Citation: European Journal of Pharmacology; 167(2): 281-90
Abstract: 125I-labelled porcine endothelin (125I-endothelin) was used to identify specific high affinity endothelin binding sites in rat cardiac membrane fragments. Binding was to a single population of sites, with a KD of 0.20 +/- 0.03 nM and a Bmax of 93.5 +/- 6.4 fmol/mg protein at 37 degrees C. Reducing the temperature to 25 degrees C increased (P less than 0.02) the KD without changing Bmax. 125I-Endothelin binding was Ca2+ independent. Specific binding was saturable and displaceable by cold endothelin and sarafotoxin S6b, but not by (-)Bay K8644, nicardipine, (-)D888, (+)cis-diltiazem, prenylamine, lidoflazine, flunarizine, nor by 10(-10)-10(-4) M CoCl2, nor 10(-10)-10(-4) M NiCl2. omega-Conotoxin, prazosin, isoprenaline, angiotensin II and its inhibitor, vasopressin and its inhibitor, glyceryl trinitrate, amiloride, ergometrine and FII stonefish toxin also failed to displace bound 125I-endothelin. 10(-4)-10(-2) M CaCl2, 10(-4)-10(-2) M MgCl2, 3 X 10(-6)-10(-3) M MnCl2, 10(-5)-3 X 10(-4) M NiCl2, and 3 X 10(-5)-3 X 10(-4) M CoCl2 stimulated the binding. Incubation at 100 degrees C for 10 min destroyed specific binding.
Internal ID Number: 2556286
URI: http://ahro.austin.org.au/austinjspui/handle/1/12562
URL: http://www.ncbi.nlm.nih.gov/pubmed/2556286
Type: Journal Article
Subjects: Animals
Binding Sites
Binding, Competitive
Cations, Divalent.pharmacology
Endothelins
Female
Hot Temperature
In Vitro Techniques
Iodine Radioisotopes.diagnostic use
Membranes.metabolism
Myocardium.metabolism
Peptides.metabolism
Rats
Rats, Inbred Strains
Receptors, Cell Surface.metabolism
Receptors, Endothelin
Swine
Appears in Collections:Journal articles

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