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
- 30 January 1989
- journal article
- Published by Wiley in FEBS Letters
- Vol. 243 (2) , 205-208
- https://doi.org/10.1016/0014-5793(89)80130-9
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°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.SCOPUS: ar.jinfo:eu-repo/semantics/publisheKeywords
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