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  • Title: Molecular architecture of secretin receptors: the specific covalent labelling of a 51 kDa peptide after cross-linking of [125I]iodosecretin to intact rat pancreatic acini.
    Author: Gossen D, Poloczek P, Svoboda M, Christophe J.
    Journal: FEBS Lett; 1989 Jan 30; 243(2):205-8. PubMed ID: 2917646.
    Abstract:
    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 degrees 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.
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