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Molecular architecture of secretin receptors: The specific covalent labelling of a 51 kDa peptide after cross‐linking of [ 125 I]iodo‐secretin to intact rat pancreatic acini
Author(s) -
Gossen Denis,
Poloczek Piotr,
Svoboda Michal,
Christophe Jean
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80130-9
Subject(s) - secretin , chemistry , peptide , biochemistry , covalent bond , reagent , receptor , labelling , pancreas , organic chemistry
p ‐Azidophenylglyoxal (APG), a heterobifunctional reagent with one group reacting selectively with arginine residues and another group photoactivable, was used to cross‐link [ 125 I]secretin prebound to intact rat pancreatic acini. The best yield was obtained when the [ 125 I]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.