Conservation of microtubule associated proteins. Isolation and characterization of tau and the high molecular weight microtubule associated protein from chicken brain and from mouse fibroblasts and comparison to the corresponding mammalian brain proteins.
Conservation of microtubule associated proteins. Isolation and characterization of tau and the high molecular weight microtubule associated protein from chicken brain and from mouse fibroblasts and comparison to the corresponding mammalian brain proteins.
复制标题
微管相关蛋白的保守。
DOI：
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发表时间：
1979
影响因子：
4.8
通讯作者：
M. Kirschner
中科院分区：
文献类型：
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作者：
D. Cleveland;B. Spiegelman;M. Kirschner
利用刺激微管蛋白组装的能力作为测定，我们在与用于分离猪脑7蛋白的条件相同的条件下纯化了鸡脑相关蛋白。鸡脑T的分子量、沉降系数和氨基酸组成与猪脑非常相似。两种r蛋白都是微异质的，并且产生非常相似和特征性的一维肽图。我们还分离了7和一个高分子量的蛋白质从猴病毒40转化的3T3细胞通过共聚标记的细胞蛋白质与载体猪脑微管。猴病毒3T3细胞蛋白与相应的猪脑相关蛋白共表达，并产生与猪蛋白模式难以区分的肽图。这些研究结果证实了7和高分子量微管相关蛋白的存在，从非神经元来源，并表明，这两个都存在于一个单一的细胞类型，如最初所建议的免疫荧光定位与抗体对猪脑蛋白。此外，从三个来源（猪脑，鸡脑，和小鼠成纤维细胞）的T多肽的相似性意味着T是一个广泛分布和保守的微管蛋白。来自猪脑和小鼠成纤维细胞的高分子量相关蛋白之间的相似性表明它们也广泛分布。
Using ability to stimulate tubulin assembly as an assay, we have purified a chicken brain associated protein under conditions identical to those used to isolate porcine brain 7 protein. Chicken brain T has a molecular weight, sedimentation coefficient, and amino acid composition very similar to porcine r. Both r proteins are microheterogeneous and yield very similar and characteristic one-dimensional peptide maps. We have also isolated 7 and a high molecular weight protein from simian virus 40-transformed 3T3 cells by copolymerization of labeled cellular proteins with carrier hog brain microtubules. The simian virus 3T3 cell proteins co-electrophorese with the corresponding hog brain associated proteins and yield peptide maps which are indistinguishable from the hog protein patterns. These findings confirm the presence of 7 and a high molecular weight microtubule associated protein from a nonneuronal source and demonstrate that both are present in a single cell type, as originally suggested by immunofluorescent localization with antibodies against the hog brain proteins. Moreover, the similarities of the T polypeptides from the three sources studied (hog brain, chicken brain, and mouse fibroblast) imply that T is a widely distributed and conserved microtubule protein. The similarities between the high molecular weight associated proteins from hog brain and mouse fibroblast suggest that they, too, are widely distributed.