Isolation of pituitary fibroblast growth factor by fast protein liquid chromatography (FPLC): Partial chemical and biological characterization

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Abstract
Bovine pituitary fibroblast growth factor has been purified 222,000‐fold to homogeneity by a combination of differential salt extraction, gel filtration, and ion exchange chromatography on Mono S column. Pituitary FGF is a single‐chain polypeptide with an apparent molecular mass of 15,800 and an isoelectric point of 9.6. It is highly active in triggering the proliferation of bovine and human vascular endothelial cell [half‐maximal stimulation at 23–40 pg/ml (1.5–2.6 pM) and saturation between 140 and 280 pg/ml (9.3–18.6 pM)]. It displays a similar activity on bovine vascular smooth muscle cells, corneal endothelial cells, granulosa and adrenal cortex cells, and rabbit costal chondrocytes.