[1,6-α-Aminosuberic acid, 3-(p-azidophenylalanine), 8-arginine] vasopressin: A new photoaffinity label for hydroosmotic hormone receptors. Characerization of the ligand and irreversible stimulation of hydroosmotic water flow in toad bladder by photoaffinity labeling

F. Fahrenholz, G. Toth, P. Crause

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

The photoreactive analog of vasopressin [1,6-α-aminosuberic acid, 3-(p-azidophenylalanine), 8-arginine] vasopressin ([Asu1,6,Phe(p-N3)3]AVP) has been synthesized. This analog retains a high binding affinity for the vasopressin receptor in plasma membranes from bovine kidney inner medulla (apparent dissociation constant, K(D) = 8.5 x 10-9 M). [Asu1,6,Phe(p-N3)3]AVP was found to be biologically active in triggering the characteristic increase in toad bladder permeability to water. Photolysis of the analog in the presence of the toad bladder results in a hydroosmotic response which persists, in spite of repeated washings, for more than 18 h. The irreversible stimulation of the bladder is inhibited when photolysis is carried out in the presence of vasopressin. Our findings indicate that with photoactivation [Asu1,6,Phe(p-N3)3]AVP binds covalently to hormonal receptors and forms an active hormone-receptor complex. This analog, therefore, is a suitable tool for studies of hydroosmotic receptor function and for receptor isolation.

Original languageEnglish
Pages (from-to)14861-14867
Number of pages7
JournalJournal of Biological Chemistry
Volume258
Issue number24
Publication statusPublished - Dec 1 1983

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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