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Characterization of glucagon‐like peptide‐I(7–36)amide receptors of rat lung membranes by covalent cross‐linking
Author(s) -
Richter Gerd,
Göke Rüdiger,
Göke Burkhard,
Schmidt Harald,
Arnold Rudolf
Publication year - 1991
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(91)80303-k
Subject(s) - adenylate kinase , membrane , receptor , chemistry , amide , ligand (biochemistry) , covalent bond , cyclase , biochemistry , peptide , organic chemistry
125 I‐labelled GLP‐I(7–36)amide was cross‐linked to a specific binding protein in rat lung membranes using disuccinimidyl suberate. A single radio‐labelled band at M r 66000 was identified by SDS‐PAGE after solubilization of the ligand‐binding protein complex which is consistent with the presence of a single class of binding sites on rat lung membranes. The band was undetectable when 1 μmol/1 GLP‐I(7–36)amide was included in the binding assay. No change in the mobility of the band was observed under reducing conditions suggesting that the binding protein in the receptor is not part of a larger disulphide‐liked protein. The intensity of the radiolabelled protein band was reduced when the incubation with 125 I‐labelled GLP‐I(7–36)amide was carried out in the presence of guanine nucleotides suggesting that the GLP‐I(7–36)amide receptor is coupled to the adenylate cyclase system.