Webb T J, Hurd H
Department of Biological Sciences, Keele University, U.K.
Insect Biochem Mol Biol. 1995 May;25(5):631-7. doi: 10.1016/0965-1748(94)00106-r.
The microsomal fraction of Tenebrio molitor follicle cells has been found to contain both high and low affinity binding sites for juvenile hormone (JH) III. Using Scatchard analysis, the equilibrium dissociation constants, Kd, were calculated as 1.0 x 10(-8) and 4.3 x 10(-7) M respectively. Kinetic data support a rapid binding of the hormone to the site(s), with rate constants of ka = 3.77 x 10(8) M-1 min-1 and kd = 0.0075 min-1. Affinity of the binding site(s) for JH III was higher than for either JH I or methoprene. The significance and possible function of such microsomal binding proteins are discussed, with reference to the perturbance of vitellogenesis found in beetles parasitized by Hymenolepis diminuta.
已发现黄粉虫卵泡细胞的微粒体部分含有对保幼激素（JH）III的高亲和力和低亲和力结合位点。使用Scatchard分析，平衡解离常数Kd分别计算为1.0×10⁻⁸和4.3×10⁻⁷M。动力学数据支持激素与该位点的快速结合，结合速率常数ka = 3.77×10⁸M⁻¹min⁻¹，kd = 0.0075min⁻¹。该结合位点对JH III的亲和力高于对JH I或烯虫酯的亲和力。参考被微小膜壳绦虫寄生的甲虫中发现的卵黄发生紊乱，讨论了这种微粒体结合蛋白的意义和可能的功能。
