从牛网膜中纯化酸性成纤维细胞生长因子。
Purification of acidic fibroblast growth factor from bovine omentum.
作者信息
Ohtaki T, Wakamatsu K, Mori M, Ishibashi Y, Yasuhara T
机构信息
Tsukuba Research Laboratories, Takeda Chemical Industries, Ltd., Ibaraki, Japan.
出版信息
Biochem Biophys Res Commun. 1989 May 30;161(1):169-75. doi: 10.1016/0006-291x(89)91576-3.
Two heparin binding growth factors with different molecular weight, 16.6 kD and 18.6 kD polypeptide, were purified from bovine omentum. The two factors have almost the same affinity to heparin; they were eluted with 1.0 M NaCl from the affinity column. The 16.6 kD polypeptide was found to be acidic fibroblast growth factor by amino acid sequence analysis. The 18.6 kD polypeptide was an N-terminus blocked polypeptide and was suggested to be beta-endothelial cell growth factor. These molecular species may play significant roles in maintaining vascularized structure in omentum and be related to the angiogenic activity of the tissue.
从牛网膜中纯化出两种分子量不同的肝素结合生长因子，即16.6 kD和18.6 kD的多肽。这两种因子对肝素的亲和力几乎相同；它们从亲和柱上用1.0 M NaCl洗脱。通过氨基酸序列分析发现16.6 kD的多肽是酸性成纤维细胞生长因子。18.6 kD的多肽是一种N端封闭的多肽，推测为β-内皮细胞生长因子。这些分子种类可能在维持网膜的血管化结构中发挥重要作用，并与该组织的血管生成活性有关。
Zotero 插件