Ho P L, Jakes R, Northrop F D, Gambarini A G
Departmento de Bioquimica, Universidade de São Paulo, Brasil.
Biochem Int. 1988 Nov;17(5):973-80.
Extraction of bovine pituitaries at pH 7.0, in the presence or absence of protease inhibitors (PMSF, leupeptin, pepstatin A and EDTA) yielded both basic and acidic FGF components that were characterized by Western blotting and sequence analysis. Basic FGF comprised several components: an 18 KDa form that is similar, if not identical, to the basic FGF (1-146) already described; a 17 KDa form that is likely to be a new truncated molecular species (11-146) and a group of immunoreactive components of about 29 KDa. Acidic FGF showed several active components of pI 4.5-6.5. The most active component has a pI of approximately 5.0; molecular weight of 17 KDa and is shown, by Western blotting, to be similar to a truncated form of bovine brain acidic FGF. The biological activity of the latter component is shown to be neutralized by anti-brain acidic FGF antiserum.
在pH 7.0条件下，无论有无蛋白酶抑制剂（苯甲基磺酰氟、亮抑酶肽、胃蛋白酶抑制剂A和乙二胺四乙酸），从牛垂体中提取的物质均产生了碱性和酸性成纤维细胞生长因子（FGF）成分，这些成分通过蛋白质免疫印迹法和序列分析进行了表征。碱性FGF包括几种成分：一种18 kDa的形式，即便不完全相同，也与已描述的碱性FGF（1 - 146）相似；一种17 kDa的形式，可能是一种新的截短分子形式（11 - 146）以及一组约29 kDa的免疫反应性成分。酸性FGF显示出几种pI为4.5 - 6.5的活性成分。活性最高的成分pI约为5.0；分子量为17 kDa，并且通过蛋白质免疫印迹法显示与牛脑酸性FGF的一种截短形式相似。后一种成分的生物活性被抗脑酸性FGF抗血清中和。
