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Abstract

Plasma membranes containing one class of high-affinity binding sites for vasopressin were prepared from bovine kidney medulla by density gradient centrifugation in Percoll. The binding affinities of reactive analogues of [Arg]vasopressin (AVP), deamino-dicarba-AVP ([1,6α-aminosuberic acid]AVP) and [2-phenylalanine]AVP to bovine antidiuretic receptor were determined. The peptide hormone analogues contained photoreactive azido or 4,4-azopentanoylamino residues or chemical reactive bromoacetylamino groups in the p position of Phe² or Phe³. All azido compounds and the bromoacetyl derivative of AVP retained high binding affinities, which is a prerequisite for specific labelling of receptors.