Characterization of glucagon‐like peptide‐I(7–36)amide receptors of rat lung membranes by covalent cross‐linking

FEBS Letters

Göke, Rüdiger¹  Arnold, Rudolf¹  Schmidt, Harald¹  Göke, Burkhard²  Richter, Gerd¹ 

[1] Department of Internal Medicine, Philipps-University of Marburg, Germany;Department of Physiology, University of Michigan, Ann Arbor, MI, USA

关键词: GLP-I(7–36)amide;    Receptor;    Lung;    Covalent cross-linking;   

DOI  :  10.1016/0014-5793(91)80303-K

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

¹²⁵I-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 ¹²⁵I-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.

【 授权许可】

Unknown