Lemke G E, Brockes J P
J Neurosci. 1984 Jan;4(1):75-83. doi: 10.1523/JNEUROSCI.04-01-00075.1984.
Cultured rat Schwann cells are stimulated to divide by a protein growth factor, present in extracts of bovine brain and pituitary, which we have named glial growth factor (GGF). Two lines of evidence indicate that GGF activity in both brain and pituitary resides in a protein of Mr = 31,000. (1) Four independently isolated monoclonal antibodies that immunoprecipitate the activity react with an antigen of this molecular weight in sodium dodecyl sulfate (SDS)-polyacrylamide gels. (2) After SDS-polyacrylamide gel electrophoresis of partially purified preparations, mitogenic activity on Schwann cells is recovered at this molecular weight. GGF has been purified approximately 10(5)-fold to apparent homogeneity from bovine pituitary anterior lobes by a combination of column chromatography steps and preparative SDS gel electrophoresis. Purified human platelet-derived growth factor, a molecule with properties similar to those of GGF, is inactive on Schwann cells and therefore appears to be distinct.
培养的大鼠雪旺细胞可被一种存在于牛脑和垂体提取物中的蛋白质生长因子刺激而分裂，我们将其命名为神经胶质生长因子（GGF）。有两条证据表明，脑和垂体中的GGF活性存在于分子量为31,000的一种蛋白质中。（1）四种独立分离的免疫沉淀该活性的单克隆抗体与十二烷基硫酸钠（SDS）-聚丙烯酰胺凝胶中这种分子量的抗原发生反应。（2）对部分纯化制剂进行SDS-聚丙烯酰胺凝胶电泳后，在该分子量处可恢复对雪旺细胞的促有丝分裂活性。通过柱色谱步骤和制备性SDS凝胶电泳相结合的方法，已从牛垂体前叶中将GGF纯化了约10⁵倍，达到了明显的均一性。纯化的人血小板衍生生长因子是一种性质与GGF相似的分子，但对雪旺细胞无活性，因此似乎是不同的。
