Ke Y Q, Fernig D G, Smith J A, Wilkinson M C, Anandappa S Y, Rudland P S, Barraclough R
Department of Biochemistry, University of Liverpool, United Kingdom.
Biochem Biophys Res Commun. 1990 Sep 28;171(3):963-71. doi: 10.1016/0006-291x(90)90778-l.
Recombinant human acidic fibroblast growth factor has been produced in E. coli cells at a level of at least 50 mg/l culture. The recombinant and natural acidic fibroblast growth factors are almost identical to one another when tested on rat mammary fibroblasts for their ability to stimulate DNA synthesis, to bind to the high-affinity surface receptors of the cells and to inhibit DNA synthesis when present in the culture medium at high concentrations. The recombinant acidic fibroblast growth factor binds to two cell-surface polypeptides of molecular masses 160 kDa and 140 kDa, which are the same size as the receptors for basic fibroblast growth factor, and it binds preferentially to the smaller polypeptide.
重组人酸性成纤维细胞生长因子已在大肠杆菌细胞中产生,产量至少为每升培养物50毫克。在对大鼠乳腺成纤维细胞进行测试时,重组酸性成纤维细胞生长因子和天然酸性成纤维细胞生长因子在刺激DNA合成的能力、与细胞高亲和力表面受体结合的能力以及在高浓度存在于培养基中时抑制DNA合成的能力方面几乎彼此相同。重组酸性成纤维细胞生长因子与分子量分别为160 kDa和140 kDa的两种细胞表面多肽结合,这两种多肽与碱性成纤维细胞生长因子的受体大小相同,并且它优先与较小的多肽结合。