Simon M, Arrigo A P, Spahr P F
Exp Cell Res. 1987 Apr;169(2):419-31. doi: 10.1016/0014-4827(87)90202-3.
Transformation of chicken embryo fibroblasts by avian retroviruses induces the tyrosine phosphorylation of a 34-39 kD cellular protein (p34). In vitro, p34 isolated from intestine interacts with F-actin in a Ca2+-dependent manner. We report here that, in the absence of Ca2+ chelators, three proteins co-purified with p34 extracted from a cytosolic or membrane fraction of chicken embryo fibroblasts; these two fractions account respectively for 10-20% and 50% of the total cellular p34. Isolated from the cytosoluble fraction of fibroblasts by sucrose gradient centrifugation and hydrophobic chromatography, p34 and the other proteins behaved as a homogeneous species upon non-denaturing gel electrophoresis, gel filtration, and CsCl density gradient centrifugation, thus indicating a strong association. Moreover, an analysis by electron microscopy following uranyl acetate staining revealed particles with a raspberry-like shape. This association was always disrupted by the calcium-chelating agent, EGTA.
禽逆转录病毒对鸡胚成纤维细胞的转化会诱导一种34 - 39 kD细胞蛋白（p34）的酪氨酸磷酸化。在体外，从肠道分离的p34以Ca2+依赖的方式与F - 肌动蛋白相互作用。我们在此报告，在不存在Ca2+螯合剂的情况下，有三种蛋白质与从鸡胚成纤维细胞的胞质或膜部分提取的p34共同纯化；这两个部分分别占细胞总p34的10 - 20%和50%。通过蔗糖梯度离心和疏水层析从成纤维细胞的可溶性部分分离得到的p34和其他蛋白质，在非变性凝胶电泳、凝胶过滤和CsCl密度梯度离心中表现为单一物种，因此表明它们有很强的结合。此外，经醋酸铀染色后的电子显微镜分析显示出类似覆盆子形状的颗粒。这种结合总是会被钙螯合剂EGTA破坏。
