Shamansky L M, Liu H Y, Hager L P, Ristic M
Mol Biochem Parasitol. 1985 Dec;17(3):299-310. doi: 10.1016/0166-6851(85)90004-0.
An 83 kDa glycoprotein and a 100 kDa glycoprotein have been purified from the supernatant fluid of in vitro cultures of Plasmodium falciparum by conventional cation-exchange liquid chromatography, size exclusion high performance liquid chromatography, and anion-exchange high performance liquid chromatography. Both proteins exist as dimers in the native state and have been identified as parasite antigens by Western immunoblotting and by their specific reactivity in the indirect enzyme-linked immunosorbent assay. The N-terminal amino acid sequence of these two proteins has been determined and they are at least 90% homologous. The use of monospecific rabbit antisera raised against the individual pure proteins confirm their cross-reactivity. We postulate that the 83 kDa protein is a specific processing product of the larger 100 kDa protein. The presence of these proteins in the culture supernatant suggests they could both be derived from the merozoite surface coat and are potential protective antigens.
通过常规阳离子交换液相色谱、尺寸排阻高效液相色谱和阴离子交换高效液相色谱，从恶性疟原虫体外培养物的上清液中纯化出了一种83 kDa糖蛋白和一种100 kDa糖蛋白。这两种蛋白质在天然状态下均以二聚体形式存在，并通过Western免疫印迹及其在间接酶联免疫吸附测定中的特异性反应被鉴定为寄生虫抗原。已确定这两种蛋白质的N端氨基酸序列，它们至少90%同源。使用针对单个纯蛋白产生的单特异性兔抗血清证实了它们的交叉反应性。我们推测83 kDa蛋白是较大的100 kDa蛋白的特定加工产物。这些蛋白质在培养上清液中的存在表明它们可能都源自裂殖子表面包膜，并且是潜在的保护性抗原。
