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Comparison of two radiolabeled quinuclidinyl benzilate ligands for the characterization of the human peripheral lung muscarinic receptor

Journal Article · · Life Sci.; (United States)

Quinuclidinyl benzilate, a muscarinic antagonist, has previously been used in its tritiated form ((/sup 3/H)-QNB) to study the lung muscarinic receptor. The authors investigated whether a newer iodinated form of QNB ((/sup 125/I)-QNB) of higher specific activity would be an appropriate ligand to study the human peripheral lung muscarinic receptor. Both the tritiated and iodinated ligands bound specifically to human lung at 23/sup 0/C. At 37/sup 0/C the specific binding of (/sup 3/H)-QNB increased slightly, but no specific binding of (/sup 125/I)-QNB was found. The data from multiple equilibrium binding experiments covering a wide range of radiolabeled QNB concentrations were combined and analyzed using the computer modeling program, LIGAND. The tritiated QNB identified a single affinity human lung binding site with a Kd of 46 +/- 9 pM. The iodinated QNB identified a single higher affinity human lung binding site of much smaller quantity. Competition studies comparing the binding of unlabeled QNB relative to labeled QNB indicated that unlabeled QNB had the same Kd as that measured for (/sup 3/H)-QNB, but a 5 log greater Kd than that measured for (/sup 125/I)-QNB. Other muscarinic receptor agonists and antagonists competed with (/sup 3/H)QNB, but not (/sup 125/I)-QNB for binding to muscarinic receptors with the expected magnitude and rank order of potency. 17 references, 2 figures, 2 tables.

Research Organization:
VA Medical Center, Iowa City, IA
DOE Contract Number:
AS05-82ER60039
OSTI ID:
6080649
Journal Information:
Life Sci.; (United States), Journal Name: Life Sci.; (United States) Vol. 41:13; ISSN LIFSA
Country of Publication:
United States
Language:
English