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A purification procedure and partial characterization of bovine pituitary fibroblast growth factor (FGF) are described. The steps of the published methods 3,4 which yield inhomogeneous material, were retained, with modifications. The final isolation, with an additional purification of approximately 20-fold, was achieved by electrophoresis in polyacrylamide gels at acid pH. The mitogenic peptide has a molecular weight of 14,500--15,000 as determined on SDS gels, chromatographs as a monomer in nondenaturing conditions, and is active at the picomolar level in effecting the incorporation of 3H-thymidine in Balb/c 3T3 cells. A preliminary amino acid composition is presented.
Lemmon et al. (1983) studied this question.