Identification and purification of glial growth factor

Identification and purification of glial growth factor
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胶质生长因子的鉴定及纯化

DOI:
10.1523/jneurosci.04-01-00075.1984
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发表时间:
1984
影响因子:
4.2
通讯作者:
J. Brockes
J. Brockes
中科院分区:
医学2区
文献类型:
--
作者:
G. Lemke;J. Brockes

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培养的大鼠雪旺细胞被刺激分裂的蛋白质生长因子,目前在提取物的牛脑和垂体,我们已经命名为胶质细胞生长因子(GGF)。两条证据表明,脑和垂体中的GGF活性存在于Mr = 31,000的蛋白质中。(1)四个独立分离的单克隆抗体,免疫沉淀的活性反应与抗原的分子量在十二烷基硫酸钠(SDS)-聚丙烯酰胺凝胶。(2)部分纯化的制剂经SDS-聚丙烯酰胺凝胶电泳后,在此分子量下恢复了对雪旺细胞的促有丝分裂活性。通过柱层析和制备型SDS凝胶电泳相结合的方法,从牛垂体前叶中纯化了约10(5)倍的GGF,达到表观均一性。纯化的人血小板衍生生长因子,一种与GGF性质相似的分子,对雪旺细胞无活性,因此似乎是不同的。
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.
DOI: 10.1002/9780470720974.ch7
发表时间: 1985
期刊: Ciba Foundation symposium
影响因子: --
作者:
R. Ross;D. Bowen-Pope;E. Raines
通讯作者: R. Ross;D. Bowen-Pope;E. Raines
从三七总皂甙和中枢神经系统中分离出的富含轴膜的组分对于培养的雪旺细胞具有促有丝分裂作用。
DOI: 10.1016/0165-3806(82)90028-1
发表时间: 1982
期刊: Brain research
影响因子: 2.9
作者:
DeVries,GH;Salzer,JL;Bunge,RP
通讯作者: Bunge,RP
DOI: --
发表时间: 1981
期刊: The Journal of biological chemistry
影响因子: --
作者:
Deuel,TF;Huang,JS;Proffitt,RT;Baenziger,JU;Chang,D;Kennedy,BB
通讯作者: Kennedy,BB