Electronic Resource
Oxford, UK
:
Blackwell Publishing Ltd
Journal of neurochemistry
47 (1986), S. 0
ISSN:
1471-4159
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Medicine
Notes:
Abstract: Reported differences in the pharmacology and distribution of [3H]nicotine and [125I]α-bungarotoxin binding sites in mammalian brain suggest that these ligands label separate receptor sites. Affinity purification of an α-bungar-otoxin binding protein from rat brain failed to copurify the high-affinity nicotine binding site, which remained in the nonbound soluble fraction after the affinity chromatogra-phy step. This confirms the independence of these putative receptor sites. Nevertheless, the binding of [125I]α-bungaro-toxin to P2 membranes was inhibited by (-)-nicotine (Ai= 9 × 10-6 M), and this sensitivity was preserved after affinity purification. It is proposed that α-bungarotoxin binds to a population of low-affinity nicotine binding sites. Comparison of the enantiomers of nicotine in competition studies at both radioligand binding sites revealed an 80-fold preference for the (-) form at the high-affinity [3H]nicotine binding site, whereas the site labelled by [125I]α-bungarotoxin displayed little stereoselectivity. In this respect, the brain α-bungarotoxin binding site resembles the nicotinic acetyl-choline receptor from Torpedo electric organ.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1471-4159.1986.tb13078.x
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