TY - JOUR
T1 - Muscarinic binding to mouse brain receptor sites
AU - Kloog, Yoel
AU - Sokolovsky, Mordechai
PY - 1978/4/14
Y1 - 1978/4/14
N2 - In mouse brain the binding of [3H]-Atropine to the muscarinic receptor seems to be a simple mass-action determined process as gauged both by approach to equilibrium kinetics and binding at equilibrium. In contrast, using isotopic dilution technique, dissociation measurements indicate the existence of two receptor-ligand complexes. It would appear that association and dissociation rates of binding of the muscarinic antagonists atropine, scopolamine, N-methyl-4-piperidyl benzilate (4NMPB) and 3-quinuclidinyl benzilate (QNB) decrease with increasing affinity based on comparisons of kinetic binding data. The differences between the association rate constants are small whereas those between the dissociation rate constants differ markedly. This kinetic behavior is similar to the well-known time profile of antimuscarinic activity in isolated tissues. These phenomena are discussed in terms of possible isomerization of the receptor-ligand complex, as has been proposed recently for [3H]-scopolamine and [3H]-4NMPB binding.
AB - In mouse brain the binding of [3H]-Atropine to the muscarinic receptor seems to be a simple mass-action determined process as gauged both by approach to equilibrium kinetics and binding at equilibrium. In contrast, using isotopic dilution technique, dissociation measurements indicate the existence of two receptor-ligand complexes. It would appear that association and dissociation rates of binding of the muscarinic antagonists atropine, scopolamine, N-methyl-4-piperidyl benzilate (4NMPB) and 3-quinuclidinyl benzilate (QNB) decrease with increasing affinity based on comparisons of kinetic binding data. The differences between the association rate constants are small whereas those between the dissociation rate constants differ markedly. This kinetic behavior is similar to the well-known time profile of antimuscarinic activity in isolated tissues. These phenomena are discussed in terms of possible isomerization of the receptor-ligand complex, as has been proposed recently for [3H]-scopolamine and [3H]-4NMPB binding.
UR - http://www.scopus.com/inward/record.url?scp=0018183742&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(78)91410-9
DO - 10.1016/0006-291X(78)91410-9
M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???
AN - SCOPUS:0018183742
SN - 0006-291X
VL - 81
SP - 710
EP - 717
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -