Sommer A, Moscatelli D, Rifkin D B
Synergen, Inc., Boulder, Colorado 80301.
Biochem Biophys Res Commun. 1989 May 15;160(3):1267-74. doi: 10.1016/s0006-291x(89)80140-8.
Basic fibroblast growth factor (bFGF) is a heparin-binding angiogenic polypeptide mitogen. bFGF proteins characteristically have a molecular weight of 18,000 which is consistent with the predicted primary translation product of 155 amino acids from the cDNA. More recently, higher molecular weight forms of bFGF have been identified but their structural relationship to the commonly known 18kD bFGFs has not been established. We now show that a 25kD bFGF purified from guinea pig brain tissue is an N-terminally extended and post-translationally modified form of the growth factor. Although the exact nature of the post-translational modifications has not been determined, circumstantial evidence suggests that they may be methylated arginines.
碱性成纤维细胞生长因子（bFGF）是一种肝素结合性血管生成多肽促分裂原。bFGF蛋白的特征分子量为18,000，这与从cDNA预测的155个氨基酸的初级翻译产物一致。最近，已鉴定出更高分子量形式的bFGF，但它们与常见的18kD bFGF的结构关系尚未确定。我们现在表明，从豚鼠脑组织中纯化的25kD bFGF是该生长因子的N端延伸且经过翻译后修饰的形式。尽管尚未确定翻译后修饰的确切性质，但间接证据表明它们可能是甲基化的精氨酸。
