Partial purification and characterization of a growth factor for macrophage progenitor cells with high proliferative potential in mouse bone marrow.

Partial purification and characterization of a growth factor for macrophage progenitor cells with high proliferative potential in mouse bone marrow.
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小鼠骨髓中具有高增殖潜力的巨噬细胞祖细胞生长因子的部分纯化和表征。

DOI:
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发表时间:
1982
期刊:
影响因子:
20.3
通讯作者:
E. Elms
E. Elms
中科院分区:
医学1区
文献类型:
--
作者:
A. Kriegler;T. Bradley;E. Januszewicz;G. Hodgson;E. Elms

文献摘要

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当新发现的生长因子(协同活性,SA)与巨噬细胞集落刺激因子(CSF)结合作为增殖刺激时,最近在体外经氟尿嘧啶处理的和正常小鼠骨髓(BM)中证实了具有高增殖潜力的巨噬细胞祖细胞群。SA,显示存在于人脾和胎盘条件培养基中(分别为HSCM和HPCM)已经被研究,并且发现对胰蛋白酶消化和在50 ℃或更高温度下加热不稳定;在pH 4和9之间稳定;不粘附于Con-A-Sepharose;并且具有pH 5 - 5.8的等电点和14,000 - 21,000的分子量,如凝胶过滤色谱所示。SA从HSCM和HPCM已被纯化89和122倍,分别通过沉淀外源蛋白在pH 5,然后在Sephacryl S200上层析两次。这些部分纯化的SA均不含小鼠BM的任何CSF。这些结果表明,来自HSCM和HPCM的SA可能是密切相关的,并且它们在结构上不同于来自各种鼠源的CSF,这些鼠源已被证明对蛋白水解酶和热稳定。
A population of macrophage progenitor cells, with high proliferative potential, has recently been demonstrated in postfluorouracil-treated and normal mouse bone marrow (BM) in vitro, when the newly discovered growth factor (synergistic activity, SA) is combined with a macrophage colony-stimulating factor (CSF) as a proliferative stimulus. SA, shown to be present in human spleen and placental conditioned media (HSCM and HPCM, respectively) have been studied and found to be unstable to trypsin digestion and to heating at 50 degrees C or above; stable between pH 4 and 9; nonadherent to Con-A-Sepharose; and to have an isoelectric point between pH 5 and 5.8 and a molecular weight of between 14,000 and 21,000 as indicated by gel filtration chromatography. SAs from both HSCM and HPCM have been purified 89- and 122-fold, respectively, by precipitation of extraneous proteins at pH 5 followed by chromatographing twice on Sephacryl S200. Neither of these partially purified SAs contain any CSF for mouse BM. These results indicate that the SAs from HSCM and HPCM may be closely related and that they are structurally different from CSFs derived from various murine sources that have been shown to be stable to proteolytic enzymes and heat.