Wiser M F, Plitt B
Max Planck Institut für Zellbiologie, Rosenhof, Ladenburg bei Heidelberg, Federal Republic of Germany.
Exp Parasitol. 1987 Dec;64(3):328-35. doi: 10.1016/0014-4894(87)90043-9.
Phosphoproteins from Plasmodium berghei, P. chabaudi, and P. falciparum are compared. A major phosphoprotein of 46 kDa is found in all three species. Peptide mapping indicates that this protein is indeed the same in all three cases and is phosphorylated at similar sites in all three species. Monoclonal antibodies were raised against three other P. berghei phosphoproteins. All three monoclonal antibodies recognize both P. berghei and P. chabaudi proteins. Only one of the monoclonal antibodies crossreacts with a P. falciparum protein of 36 kDa, whereas the equivalent P. berghei and P. chabaudi proteins are 34 and 32 kDa, respectively. The highest rate of synthesis of the phosphoproteins is observed during the early trophozoite stage, whereas the highest rate of phosphorylation is observed during the late trophozoite stage.
对来自伯氏疟原虫、查巴迪疟原虫和恶性疟原虫的磷蛋白进行了比较。在所有这三个物种中都发现了一种主要的46 kDa磷蛋白。肽图谱分析表明，该蛋白在所有三种情况下确实相同，并且在所有三个物种的相似位点被磷酸化。针对伯氏疟原虫的另外三种磷蛋白制备了单克隆抗体。所有三种单克隆抗体都能识别伯氏疟原虫和查巴迪疟原虫的蛋白。只有一种单克隆抗体与一种36 kDa的恶性疟原虫蛋白发生交叉反应，而伯氏疟原虫和查巴迪疟原虫的等效蛋白分别为34 kDa和32 kDa。磷蛋白的合成速率在滋养体早期阶段最高，而磷酸化速率在滋养体后期阶段最高。
