Dagger F, Dunia I, Hernandez A G, Pradel L A, Benedetti E L
Department of Cell Biology, Faculty of Sciences, Universidad Central de Venezuela, Caracas.
Mol Biol Rep. 1988;13(4):197-206. doi: 10.1007/BF00788171.
The presence and the localization of actin, spectrin and ankyrin are studied by immunofluorescence and immunoblotting in Leishmania mexicana promastigotes growing in vitro. These proteins, amphitropic in nature, coexist both in soluble and insoluble forms. Our results demonstrate that the Triton insoluble form of these proteins constitutes beside tubulin the cytoskeletal scaffold of promastigotes in close association with the plasma membrane, the axoneme and the basal body of the parasite.
通过免疫荧光和免疫印迹法研究了体外生长的墨西哥利什曼原虫前鞭毛体中肌动蛋白、血影蛋白和锚蛋白的存在及定位。这些蛋白质本质上具有两性,以可溶性和不溶性两种形式共存。我们的结果表明,这些蛋白质的Triton不溶性形式除微管蛋白外,构成了前鞭毛体的细胞骨架支架,与寄生虫的质膜、轴丝和基体紧密相连。