Characterization of the detergent solubilized receptor for gastrin-releasing peptide

D. Cirillo, L. Naldini, T. W. Moody, P. Comoglio, J. Schlessinger, R. Kris

Research output: Contribution to journalArticlepeer-review


Properties of detergent solubilized gastrin-releasing peptide receptor were investigated. Swiss 3T3 membranes were covalently labeled with [125I]GRP and homobifunctional cross-linkers. A major labeled protein of 75 kDa was resolved using SDS-polyacrylamide gel electrophoresis. When the same preparation was solubilized with zwitterionic detergent and analyzed under nondenaturing conditions the protein bound radioactivity was resolved in two different peaks, a major one of apparent molecular weight 220,000 (peak 1) and a minor one of 80,000 (peak 2) both containing the 75 kDa protein. Specific ligand binding activity also eluted with peak 1. These results indicate that the active form of bombesin/GRP receptor is a large complex containing the 75 kDa ligand binding domain.

Original languageEnglish
Pages (from-to)737-745
Number of pages9
Issue number4
Publication statusPublished - 1990


  • Gastrin-releasing peptide
  • Neuropeptide
  • Peptide
  • Receptor
  • Solubilization

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Physiology
  • Cellular and Molecular Neuroscience


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