Miroshnikov A I, Boĭkov V A, Snezhkova L G, Severin S E, Shvets V I
Bioorg Khim. 1983 Jan;9(1):26-32.
Tertiapin, a neurotoxin from the honey bee venom, interacts specifically with calmodulin in the presence of Ca2+. The nature of this interaction was studied using calmodulin-cAMP phosphodiesterase system. Tertiapin does not affect the unstimulated basal activity of phosphodiesterase. However, it totally inhibits the enzyme-activating capacity of calmodulin. Analysis of the dose-dependent activation of phosphodiesterase by calmodulin in the presence of tertiapin indicated that inhibition is caused by the interaction of two tertiapin molecules with calmodulin (Kd 2 microM). The data obtained suggest that the toxic effect of tertiapin in nervous tissue is mediated by blockade of calmodulin function.
蜂毒中的神经毒素蜂毒明肽(Tertiapin)在Ca2+存在的情况下与钙调蛋白特异性相互作用。利用钙调蛋白 - cAMP磷酸二酯酶系统研究了这种相互作用的性质。蜂毒明肽不影响磷酸二酯酶未受刺激的基础活性。然而,它完全抑制了钙调蛋白的酶激活能力。在蜂毒明肽存在的情况下,对钙调蛋白对磷酸二酯酶的剂量依赖性激活分析表明,抑制是由两个蜂毒明肽分子与钙调蛋白的相互作用引起的(解离常数Kd为2 microM)。所获得的数据表明,蜂毒明肽在神经组织中的毒性作用是通过阻断钙调蛋白的功能介导的。