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Characterisation of a high‐affinity VIP receptor in human lung parenchyma
Author(s) -
Schachter M.,
Dickinson K.E.J.,
Miles C.M.,
Sever P.S.
Publication year - 1986
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(86)81237-6
Subject(s) - vasoactive intestinal peptide , kinetics , chemistry , receptor , secretin , glucagon , receptor–ligand kinetics , potency , biophysics , binding site , membrane , stereochemistry , endocrinology , medicine , biochemistry , biology , neuropeptide , in vitro , pancreas , hormone , quantum mechanics , physics
A method is described for preparing human lung parenchymal membranes essentially free of carbon contamination. Using this technique, a high‐affinity 125 I‐VIP‐binding site has been characterised. The receptor density is approx. 200 protein and the K d of 125 I‐VIP by saturation binding is 200 pM. The dissociation kinetics are complex and cannot be described by first‐order kinetics. Several VIP‐related peptides displace 125 I‐VIP from this binding site with a rank order of potency: VIP > rat GRF > PHM> PHI > human GRF>secretin>glucagon. Displacement curves of these peptides exhibited slope factors significantly less than unity with the exception of human GRF.