PRIMARY STRUCTURE OF BOVINE PITUITARY BASIC FIBROBLAST GROWTH-FACTOR (FGF) AND COMPARISON WITH THE AMINO-TERMINAL SEQUENCE OF BOVINE BRAIN ACIDIC FGF
PRIMARY STRUCTURE OF BOVINE PITUITARY BASIC FIBROBLAST GROWTH-FACTOR (FGF) AND COMPARISON WITH THE AMINO-TERMINAL SEQUENCE OF BOVINE BRAIN ACIDIC FGF
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DOI：
10.1073/pnas.82.19.6507
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发表时间：
1985-01-01
影响因子：
11.1
通讯作者：
GUILLEMIN, R
中科院分区：
文献类型：
--
作者：
ESCH, F;BAIRD, A;GUILLEMIN, R
内皮细胞的两种主要促有丝分裂多肽已被纯化至均一。用气相序列分析法测定了牛垂体碱性成纤维细胞生长因子（FGF）的完整一级结构和牛脑酸性FGF的氨基端氨基酸序列。这些多肽的均质制剂是有效的促有丝分裂剂（碱性FGF，ED 50 approxeq. 60 μ g/ml;酸性FGF ED 50 6000 pg/ml）;在体内，碱性FGF在鸡绒毛尿囊膜测定中是一种强有力的血管生成剂。可用的蛋白质序列数据证明两种多肽之间存在显著的结构同源性。
The two major mitogenic polypeptides for endothelial cells have been purified to homogeneity. The complete primary structure of bovine pituitary basic fibroblast growth factor (FGF) and the amino-terminal amino acid sequence of bovine brain acidic FGF have been established by gas-phase sequence analyses. Homogeneous preparations of these polypeptides are potent mitogens (basic FGF, ED50 .apprxeq. 60 pg/ml; acidic FGF ED50 .apprxeq. 6000 pg/ml) for many diverse cell types including capillary endothelial cells, vascular smooth muscle cells, and adrenocortical and granulosa cells; in vivo, basic FGF is a powerful angiogenic agent in the chick chorioallantoic membrane assay. The available protein sequence data demonstrate the existence of significant structural homology between the two polypeptides.