• Citer

Molecular architecture of secretin receptors: The specific covalent labelling of a 51 kDa peptide after cross-linking of [125I]iodo-secretin to intact rat pancreatic acini

par Gossen, Denis ;Poloczek, Piotr ;Svoboda, Michal ;Christophe, Jean
Référence FEBS letters, 243, 2, page (205-208)
Publication Publié, 1989

Article révisé par les pairs

• Accès en ligne
• Détails
• Contenu
• Statistiques

Résumé :

p-Azidophenylglyoxal (APG), a heterobifunctional reagent with one group reacting selectively with arginine residues and another group photoactivable, was used to cross-link [125I]secretin prebound to intact rat pancreatic acini. The best yield was obtained when the [125I]secretin-acini complex was incubated under dim light with 2 mM APG at 37°C and pH 8.0, followed by photolysis at 312 nm. The main secretin binding peptide cross-linked under reducing conditions, when tested by SDS-PAGE and autoradiography: (i) had a molecular mass of 51 kDa and was not a subunit of a larger, disulfide-linked structure, and (ii) was distinct from the main VIP binding peptide coexisting in the same preparation.