Buranakitjaroen P, Newbold C I
Mol Biochem Parasitol. 1987 Jan 2;22(1):65-77. doi: 10.1016/0166-6851(87)90070-3.
A monoclonal antibody raised against merozoites of Plasmodium falciparum clone T9/96 was shown to react with an extremely strain specific epitope on a 195 kDa protein synthesized only by late trophozoites and schizonts. This protein was shown to exhibit all of the characteristics attributed to the molecule known variously as merozoite surface protein precursor, polymorphic schizont antigen and p195. The monoclonal antibody also identified a cross-reactive epitope on a distinct protein of 100 kDa in ring stage parasites which was shown to be synthesized throughout the asexual cycle and was not a processing product of p195. One-dimensional peptide mapping studies suggested that these two proteins share a degree of common sequence or structure.
一种针对恶性疟原虫克隆T9/96裂殖子产生的单克隆抗体，被证明能与仅由晚期滋养体和裂殖体合成的195 kDa蛋白上的一个极具菌株特异性的表位发生反应。该蛋白表现出了各种被认为是裂殖子表面蛋白前体、多态性裂殖体抗原和p195等分子所具有的所有特征。该单克隆抗体还在环状体期寄生虫的一种不同的100 kDa蛋白上识别出一个交叉反应表位，该蛋白在整个无性周期中都有合成，且不是p195的加工产物。一维肽图谱研究表明，这两种蛋白具有一定程度的共同序列或结构。
