Suetterlin B W, Kappes B, Franklin R M
Biocenter, Department of Structural Biology, Basel, Switzerland.
Mol Biochem Parasitol. 1991 May;46(1):113-22. doi: 10.1016/0166-6851(91)90205-k.
Fifty-nine Plasmodium falciparum specific phosphoproteins with molecular weights between 15,000 and 192,000 were analyzed by SDS-PAGE and two-dimensional gel electrophoresis. 40 phosphoproteins were identified by [gamma-32P]ATP labeling of cell lysates, 19 by [32P]orthophosphate labeling of parasitic cultures in vivo. Changes in the phosphorylation pattern during the infectious erythrocytic cycle were determined for all proteins. In parallel, cell fractionation studies were done to follow up possible changes in the cellular distribution of these proteins. Several phosphoproteins are associated with the membrane fraction of infected erythrocytes. One pair of proteins of approx. 88 kDa and a pI of about 5.0 was further characterized. Both proteins are located in the parasitic fractions as well as in the membrane of infected erythrocytes during the entire cycle. Phosphorylation of these proteins, however, is restricted to the trophozoite and schizont stages. Peptide mapping studies demonstrated that both proteins are identical with the exception of minor modifications which are probably not the result of differences in phosphorylation.
通过SDS - PAGE和二维凝胶电泳分析了59种分子量在15,000至192,000之间的恶性疟原虫特异性磷蛋白。通过细胞裂解物的[γ-32P]ATP标记鉴定了40种磷蛋白，通过体内寄生虫培养物的[32P]正磷酸盐标记鉴定了19种。确定了所有蛋白质在感染性红细胞周期中的磷酸化模式变化。同时，进行了细胞分级分离研究，以追踪这些蛋白质细胞分布的可能变化。几种磷蛋白与感染红细胞的膜部分相关。进一步表征了一对分子量约为88 kDa、pI约为5.0的蛋白质。在整个周期中，这两种蛋白质都位于寄生虫部分以及感染红细胞的膜中。然而，这些蛋白质的磷酸化仅限于滋养体和裂殖体阶段。肽图谱研究表明，这两种蛋白质除了可能不是磷酸化差异导致的微小修饰外是相同的。
