Two distinct (-)nicotine binding sites in goldfish brain. Identification and characterization of putative neuronal nicotinic acetylcholine receptor subtypes.
作者： J M Henley , R E Oswald
DOI: 10.1016/S0021-9258(18)48297-X
关键词: Stereoisomerism 、 Sepharose 、 Nicotine 、 Binding site 、 Nicotinic acetylcholine receptor 、 Chemistry 、 Receptor 、 Binding protein 、 Acetylcholine receptor 、 Biochemistry
摘要: The binding of (-)-[3H]nicotine to membrane fragments and a detergent solubilized fraction goldfish brain was characterized. not displaced by alpha-bungarotoxin, but (-)nicotine carbamoylcholine with Ki approximately 8.6 86 nM, respectively. Preincubation extract alpha-bungarotoxin-coupled Sepharose resulted in the loss 50% protein from eluent an increase gel compared control, non-alpha-bungarotoxin Sepharose. 125I-alpha-bungarotoxin same preincubation experiments totally removed. In addition, incubation tissue extracts affinity for (mean KD = 3.1) control (KD 6.4 nM). Specific sites could be eluted D-tubocurarine. Similar previously reported data, eye removal 40% decrease contralateral tectum that ipsilateral tectum. These data indicate at least two distinct subtypes may present brain, one which binds alpha-bungarotoxin another only (-)nicotine.
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