Trotter J L, Lieberman L, Margolis F L, Agrawal H C
J Neurochem. 1981 Mar;36(3):1256-62. doi: 10.1111/j.1471-4159.1981.tb01725.x.
A double-antibody radioimmunoassay (RIA) has been developed with antisera to purified rat brain myelin proteolipid protein (PLP). The addition of Triton X-100 allowed antibody-antigen interaction and immune precipitation in the presence of sodium dodecyl sulfate (SDS). The RIA will accurately measure 8-80 ng of PLP in buffer or human serum. The RIA is highly specific for myelin PLP and does not cross-react with material in tissues (heart, kidney, muscle, testicle, and intestine) other than the central nervous system. The antibodies to rat myelin PLP cross-react with PLP from bovine brain homogenate or myelin. Myelin PLP was found to account for 55 and 52% of total myelin protein from bovine and rat brain, respectively. Furthermore, there is a higher concentration of PLP in white than in gray matter corresponding to the degree of myelination. Unlike myelin basic protein, myelin PLP was undetectable in both bovine and rat peripheral nervous system.
已利用针对纯化的大鼠脑髓鞘蛋白脂蛋白（PLP）的抗血清开发出一种双抗体放射免疫分析（RIA）方法。添加 Triton X - 100 可在十二烷基硫酸钠（SDS）存在的情况下实现抗体 - 抗原相互作用和免疫沉淀。该 RIA 能够准确测量缓冲液或人血清中 8 - 80 ng 的 PLP。该 RIA 对髓鞘 PLP 具有高度特异性，并且不会与中枢神经系统以外的组织（心脏、肾脏、肌肉、睾丸和肠道）中的物质发生交叉反应。针对大鼠髓鞘 PLP 的抗体与来自牛脑匀浆或髓鞘的 PLP 发生交叉反应。发现髓鞘 PLP 分别占牛脑和大鼠脑总髓鞘蛋白的 55%和 52%。此外，白质中 PLP 的浓度高于灰质，这与髓鞘形成程度相对应。与髓鞘碱性蛋白不同，在牛和大鼠的外周神经系统中均未检测到髓鞘 PLP。
