Maitre M, Rumigny J F, Mandel P
Neurochem Res. 1983 Jan;8(1):113-20. doi: 10.1007/BF00965658.
High affinity binding sites for gamma-hydroxybutyrate have recently been shown to exist on crude membranes of rat brain. These sites exhibit a dissociation constant of 95 nM and a capacity of 557 fentomoles per mg protein. However, after more extensive washing of the crude membrane fraction and performing binding experiments at a lower concentration of radioactive GHB (below 20 nM), the existence of another binding site for GHB with a higher affinity than previously described was discovered. The data concerning this binding site are in favour of positive cooperative binding characteristics. This binding site may play a role in the mediation of the multiple physiological and pharmacological effects of GHB in the rat CNS and its presence provides additional evidence in favour of a neuromodulator or neurotransmitter role of GHB.
最近已证明，大鼠脑粗膜上存在γ-羟基丁酸的高亲和力结合位点。这些位点的解离常数为95 nM，每毫克蛋白质的容量为557飞摩尔。然而，在对粗膜部分进行更广泛的洗涤并在较低浓度的放射性γ-羟基丁酸（低于20 nM）下进行结合实验后，发现了另一个对γ-羟基丁酸具有比先前描述更高亲和力的结合位点。有关此结合位点的数据支持正协同结合特性。该结合位点可能在介导γ-羟基丁酸在大鼠中枢神经系统中的多种生理和药理作用中发挥作用，其存在为γ-羟基丁酸作为神经调节剂或神经递质的作用提供了额外证据。
