Characterization of a high affinity piretanide receptor on kidney membranes |
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Authors: | E M Giesen-Crouse C Welsch J L Imbs M Schmidt J Schwartz |
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Affiliation: | 1. University Department of Ophthalmology, Zagreb University Hospital Center, Zagreb, Croatia;2. Department of Anatomy and Neuroscience, School of Medicine, University of Osijek, Osijek, Croatia;3. Department of Pharmacology, School of Medicine, University of Zagreb, Zagreb, Croatia;4. Department of Pathology, School of Medicine, University of Zagreb, Zagreb, Croatia;5. University Department of Ophthalmology, Sestre Milosrdnice University Hospital Center, Zagreb, Croatia;1. Macromolecules and Interfaces Institute, Virginia Tech, Blacksburg, VA 24061, USA;2. Department of Sustainable Biomaterials, Virginia Tech, Blacksburg, VA 24061, USA;3. Department of Chemistry, Biochemistry and Physics, Niagara University, Lewiston, NY 14109, USA;4. Department of Chemistry, Virginia Tech, Blacksburg, VA 24061, USA;1. Mathematical Sciences Institute, Australian National University, Acton, ACT 2601, Australia;2. Department of Theoretical Physics, Research School of Physics and Engineering, and Mathematical Sciences Institute, Australian National University, Acton, ACT 2601, Australia |
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Abstract: | The tritiated loop diuretic, piretanide, is a useful ligand for specific diuretic receptors which are present in the plasma membranes of renal medullary cells. Its high specific activity (30 Ci X mmol-1) made it possible to demonstrate the existence of a high affinity receptor (Kd approximately 5 nM) and a binding site with low affinity. High affinity binding is saturable, reversible and displaceable by a number of non-radioactive loop diuretics. Structural analogues, devoid of diuretic activity, do not displace piretanide binding. No specific binding occurs in liver or spleen membranes. |
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