Neumeier R, Maurer H R
Hoppe Seylers Z Physiol Chem. 1982 Dec;363(12):1493-500. doi: 10.1515/bchm2.1982.363.2.1493.
A high molecular mass type of granulocyte colony-stimulating factor (CSF-F) from bovine lung tissue produced by fibroblasts was isolated and partially purified by a four-step procedure. Following ammonium sulfate fractionation, hydrophobic interaction, ion-exchange and affinity chromatography, CSF-F was more than 200-fold enriched. CSF-F was found to be a glycoprotein of approximately 68 kDa with an isoelectric point of 4.0-5.2. It did not lose its biological activity after neuraminidase treatment. Gel-filtration behavior of desialo-CSF-F was not changed.
通过成纤维细胞产生的来自牛肺组织的一种高分子量类型的粒细胞集落刺激因子(CSF-F),经四步程序进行分离和部分纯化。经过硫酸铵分级分离、疏水相互作用、离子交换和亲和层析后,CSF-F的富集倍数超过200倍。发现CSF-F是一种约68 kDa的糖蛋白,等电点为4.0 - 5.2。经神经氨酸酶处理后其生物活性未丧失。去唾液酸CSF-F的凝胶过滤行为未改变。