Pong S S, Wang C C
J Neurochem. 1982 Feb;38(2):375-9. doi: 10.1111/j.1471-4159.1982.tb08639.x.
Avermectin B1a stimulates high-affinity binding of [3H]-gamma-aminobutyric acid (GABA) to receptors in washed rat brain membranes. Scatchard analysis of the data indicates that the drug does not significantly alter the apparent dissociation constant of GABA binding, but increases the detectable number of binding sites from 3.2 to 5.1 pmol/mg protein, (+)-Bicuculline completely blocks control and avermectin B1a-stimulated GABA binding, whereas picrotoxin antagonizes specifically the avermectin B1a-stimulated GABA binding. The avermectin B1a-stimulated GABA binding is also chloride ion-dependent, whereas GABA binding in the control is not. These observations suggest that the mechanism of avermectin B1a stimulation of GABA binding may involve the chloride ion channel.
阿维菌素B1a刺激[3H]-γ-氨基丁酸（GABA）与经洗涤的大鼠脑膜中的受体的高亲和力结合。对数据的Scatchard分析表明，该药物不会显著改变GABA结合的表观解离常数，但会将可检测到的结合位点数量从3.2皮摩尔/毫克蛋白质增加到5.1皮摩尔/毫克蛋白质，（+）-荷包牡丹碱完全阻断对照和阿维菌素B1a刺激的GABA结合，而印防己毒素则特异性拮抗阿维菌素B1a刺激的GABA结合。阿维菌素B1a刺激的GABA结合也依赖于氯离子，而对照中的GABA结合则不依赖。这些观察结果表明，阿维菌素B1a刺激GABA结合的机制可能涉及氯离子通道。
