PURIFICATION AND CHARACTERIZATION OF HUMAN GRANULOCYTE COLONY-STIMULATING FACTOR (G-CSF)
PURIFICATION AND CHARACTERIZATION OF HUMAN GRANULOCYTE COLONY-STIMULATING FACTOR (G-CSF)
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DOI：
10.1002/j.1460-2075.1986.tb04297.x
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发表时间：
1986-05-01
期刊：
影响因子：
11.4
通讯作者：
ASANO, S
中科院分区：
文献类型：
--
作者：
NOMURA, H;IMAZEKI, I;ASANO, S
一种集落刺激因子(CSF)已经从产生集落刺激因子的人肿瘤细胞系CHU-2的无血清培养上清中纯化到均一。该分子为疏水性糖蛋白(摩尔数)。WT 19,000，pI=6.1为asialo形式)，可能含有O-连接的糖苷。对该分子进行氨基酸序列测定，得到单一的NH2末端序列，与以前报道的其他CSF的相应序列没有同源性。其生物学活性明显是人和小鼠骨髓细胞的中性粒细胞系所特有的，比活性为2.7倍。108个集落/105个非贴壁人骨髓细胞/mg蛋白。纯化的脑脊液可作为人源性粒细胞集落刺激因子，可作为研究人类粒细胞生成调控机制的有用材料。
A colony-stimulating factor (CSF) has been purified to homogeneity from the serum-free medium conditioned by one of the human CSF-producing tumor cell lines, CHU-2. The molecule was a hydrophobic glycoprotein (mol. wt 19,000, pI = 6.1 as asialo form) with possible O-linked glycosides. Amino acid sequence determination of the molecule gave a single NH2-terminal sequence which had no homology to the corresponding sequence of the other CSFs previously reported. The biological activity was apparently specific for a neutrophilic granulocyte-lineage of both human and mouse bone marrow cells with a specific activity of 2.7 .times. 108 colonies/105 non-adherent human bone marrow cells/mg protein. The purified CSF can be regarded as a G-CSF of human origin and will become a useful material for investigation of regulatory mechanisms of human granulopoiesis.