SP-40,40的β-内啡肽结合活性。
Beta-endorphin binding activity of SP-40,40.
作者信息
Choi-Miura N H, Nakano Y, Tobe T, Mazda T, Tomita M
机构信息
Department of Physiological Chemistry, School of Pharmaceutical Sciences, Showa University, Tokyo, Japan.
出版信息
Biol Pharm Bull. 1993 Mar;16(3):228-31. doi: 10.1248/bpb.16.228.
SP-40,40 bound to beta-endorphin via C-terminal non-opioid portion of beta-endorphin as well as S-protein (vitronectin) bound. Beta-endorphin bound mainly to SP-40,40, but not to S-protein, in the soluble membrane attack complex (SMAC, SC5b-9) of complement, because the results of autoradiography of the cross-linking experiment of SMAC with [125I] beta-endorphin revealed only a typical band of SP-40,40. The binding of SP-40,40 to beta-endorphin inhibited the binding of beta-endorphin to its receptor of rat brain; thus SP-40,40 might inhibit the biological action of beta-endorphin.
SP-40,40 通过β-内啡肽的 C 末端非阿片样部分与β-内啡肽结合，同时也与 S 蛋白（玻连蛋白）结合。在补体的可溶性膜攻击复合物（SMAC，SC5b-9）中，β-内啡肽主要与 SP-40,40 结合，而不与 S 蛋白结合，因为用[125I]β-内啡肽对 SMAC 进行交联实验的放射自显影结果仅显示出一条典型的 SP-40,40 条带。SP-40,40 与β-内啡肽的结合抑制了β-内啡肽与大鼠脑内其受体的结合；因此，SP-40,40 可能会抑制β-内啡肽的生物学作用。
Zotero 插件