Goncharova V P, Eropkin M Iu, Chalisova N I, Akoev G N, Eropkina E M, Shevchenko A A
Tsitologiia. 1991;33(2):67-75.
An acid-soluble protein was isolated from bovine brain tissue using a combination of 5% HClO4 acidic extraction, cation-exchange chromatography and heparin-Sepharose affinity chromatography. This preparation had a biological activity similar to that of the fibroblast growth factor (FGF). It has stimulated neurite outgrowth in organotypic culture of chicken embryo dorsal root ganglia and also has stimulated a proliferation of human embryonic fibroblasts in the culture. The biological activity of isolated preparation was totally inhibited by anti-bFGF antibodies, while anti-aFGF antibodies had no effect. The bFGF showed a neurite stimulating activity in the organotypic culture that was completely abolished by the anti-bFGF, IgG, while the aFGF was inactive. This data, as well as cationic properties of isolated protein and its heparin-binding ability, enable us to postulate a high degree of homology of the brain acid-soluble protein and the bFGF. At the same time the relations of the isolated growth factor and other brain-derived heparin-binding growth factors are yet to be established.
使用5%高氯酸酸性提取、阳离子交换色谱法和肝素-琼脂糖亲和色谱法相结合的方法，从牛脑组织中分离出一种酸溶性蛋白。该制剂具有与成纤维细胞生长因子（FGF）相似的生物活性。它在鸡胚背根神经节的器官型培养中刺激了神经突生长，并且在培养中也刺激了人胚胎成纤维细胞的增殖。分离制剂的生物活性被抗bFGF抗体完全抑制，而抗aFGF抗体则没有作用。bFGF在器官型培养中显示出神经突刺激活性，该活性被抗bFGF IgG完全消除，而aFGF则无活性。这些数据，以及分离蛋白的阳离子特性及其肝素结合能力，使我们能够推测脑酸溶性蛋白与bFGF具有高度同源性。同时，分离出的生长因子与其他脑源性肝素结合生长因子之间的关系尚待确定。
