Purification and partial characterization of bovine pituitary fibroblast growth factor
Purification and partial characterization of bovine pituitary fibroblast growth factor
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牛垂体成纤维细胞生长因子的纯化和部分表征
DOI：
10.1002/jcb.240210302
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发表时间：
1983
影响因子：
4
通讯作者：
R. Bradshaw
中科院分区：
文献类型：
--
作者：
S. Lemmon;R. Bradshaw
描述了牛垂体成纤维细胞生长因子（FGF）的纯化过程和部分特性。保留了已发表的方法[3,4]中产生非均匀材料的步骤，并进行了修改。最后的分离，额外的纯化约20倍，是在酸性的聚丙烯酰胺凝胶中通过电泳实现的。有丝分裂肽在SDS凝胶上测定的分子量为14,500 - 15,000，在非变性条件下作为单体的色谱，在皮摩尔水平上影响3H胸腺嘧啶在Balb/c 3T3细胞中的结合。提出了初步的氨基酸组成。
A purification procedure and partial characterization of bovine pituitary fibroblast growth factor (FGF) are described. The steps of the published methods [3,4] which yield inhomogeneous material, were retained, with modifications. The final isolation, with an additional purification of ∼20‐fold, was achieved by electro‐phoresis in polyacrylamide gels at acid pH. The mitogenic peptide has a molecular weight of 14,500–15,00 as determined on SDS gels, chromatographs as a monomer in nondenaturing conditions, and is active at the picomolar level in effecting the incorporation of 3H‐thymidine in Balb/c 3T3 cells. A preliminary amino acid composition is presented.