Purification in high yield of brain fibroblast growth factor by preparative isoelectric focusing at pH 9.6.

The purification of fibroblast growth factor (FGF) from bovine brain has been reported (Gospodarowicz, D., Bialecki, H., and Greenburg G. (1978) J. Biol. Chem. 253, 3736-3743). Further studies have shown that bovine brain fibroblast growth factor is composed of three fragments derived by limited proteolysis from myelin basic protein (Westall, F. C., Lennon, V. A., and Gospodarowicz, D. (1978) Proc. Natl. Acad. Sci. U. S. A. 75, 4675-4678). Two of these fragments (FGF-1 and -2) had a high specific mitogenic activity. In the presence study, we have used isoelectric focusing to purify brain FGF to homogeneity. The principal active components of brain FGF preparations partially purified by gel filtration on Sephadex G-75 can be recovered in high yield from isoelectric focusing in sucrose. These components have a pI of 9.6 and 9.54, respectively. Their electrophoretic mobility, amino acid composition, and biological properties are identical with those previously reported for FGF-1 and -2.