Purification and partial characterization of bovine pituitary fibroblast growth factor.
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.
D000596:Amino Acids / Q000032:analysis; D000645:Ammonium Sulfate; D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D003956:Dialysis; D004589:Electrophoresis, Disc; D004591:Electrophoresis, Polyacrylamide Gel; D005346:Fibroblast Growth Factors / Q000302:isolation & purification*; D051379:Mice; D008807:Mice, Inbred BALB C; D010902:Pituitary Gland / Q000032:analysis*; D013936:Thymidine / Q000378:metabolism
D000596:Amino Acids; D005346:Fibroblast Growth Factors; D000645:Ammonium Sulfate; D013936:Thymidine