Properties of a high affinity binding site for [3H]avermectin B1a.
Properties of a high affinity binding site for [3H]avermectin B1a.
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[3H]阿维菌素 B1a 高亲和力结合位点的特性。
DOI：
10.1016/0014-2999(84)90133-x
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发表时间：
1984
影响因子：
5
通讯作者：
W. Sieghart
中科院分区：
文献类型：
--
作者：
G. Drexler;W. Sieghart
研究了[3H]阿维菌素B1a在大鼠几个脑区膜上的特异性高亲和力结合。结合发生迅速，是可逆的，部分依赖于氯离子在孵育介质中的存在。GABA受体激动剂可部分抑制[3H]阿维菌素B1a的特异性高亲和力结合，而GABA受体拮抗剂可阻断这种作用。戊巴比妥和依唑酸盐抑制了[3H]阿维菌素B1a的高亲和力结合，而picrotoxin、picrotoxin和IPTBO则刺激了[3H]阿维菌素B1a的高亲和力结合。所有这些效应都受到孵育介质中氯离子存在的影响。结果表明，[3H]阿维菌素B1a的高亲和力结合位点与gaba -苯二氮卓受体-氯离子通道复合物有关。
The specific high affinity binding of [3H]avermectin B1a was investigated in membranes from several rat brain regions. Binding occured rapidly, was reversible and partially dependent on the presence of chloride ions in the incubation medium. Specific high affinity binding of [3H]avermectin B1a was partially inhibited by GABA receptor agonists and this effect was blocked by GABA receptor antagonists. Pentobarbital and etazolate inhibited, and picrotoxin, picrotoxinin and IPTBO stimulated high affinity binding of [3H]avermectin B1a. All these effects were influenced by the presence of chloride ions in the incubation medium. The results indicate that the high affinity binding site of [3H]avermectin B1a is associated with the GABA-benzodiazepine receptor-chloride ion channel complex.