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从牛脑中纯化成纤维细胞生长因子活性物质。

Purification of the fibroblast growth factor activity from bovine brain.

作者信息

Gospodarowicz D, Bialecki H, Greenburg G

出版信息

J Biol Chem. 1978 May 25;253(10):3736-43.

PMID:649600
Abstract

The purification of the fibroblast growth factor (FGF) from bovine brain has led to the isolation of two peptides. FGF-1 with 128 amino acids and FGF-2 with 107 amino acids. The biological activity of these two peptides is acid- and heat-labile. As indicated by the amino acid composition of FGF-1 and -2, these two peptides are derived from a common precursor and bear no resemblance to pituitary FGF. The brain FGF peptides, like pituitary FGF, are mitogenic in vitro for the same wide variety of mesoderm-derived cells. Since their mitogenic activity is acid- and heat-labile, they are thereby distinguished from the platelet factor isolated from platelets and from the cationic peptide isolated from serum which has been shown to have the same molecular weight and isoelectric point as brain and pituitary FGF.

摘要

从牛脑中纯化成纤维细胞生长因子(FGF)已导致两种肽的分离。含128个氨基酸的FGF-1和含107个氨基酸的FGF-2。这两种肽的生物活性对酸和热不稳定。正如FGF-1和-2的氨基酸组成所示,这两种肽源自一个共同的前体,与垂体FGF没有相似之处。脑FGF肽与垂体FGF一样,在体外对多种中胚层来源的细胞具有促有丝分裂作用。由于它们的促有丝分裂活性对酸和热不稳定,因此它们与从血小板中分离的血小板因子以及从血清中分离的阳离子肽不同,后者已被证明与脑和垂体FGF具有相同的分子量和等电点。

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