Primary structure of bovine pituitary basic fibroblast growth factor (FGF) and comparison with the amino-terminal sequence of bovine brain acidic FGF

Proc Natl Acad Sci U S A. 1985 Oct;82(19):6507-11. doi: 10.1073/pnas.82.19.6507.

Abstract

The two major mitogenic polypeptides for endothelial cells have been purified to homogeneity. The complete primary structure of bovine pituitary basic fibroblast growth factor (FGF) and the amino-terminal amino acid sequence of bovine brain acidic FGF have been established by gas-phase sequence analyses. Homogeneous preparations of these polypeptides are potent mitogens (basic FGF, ED50 approximately equal to 60 pg/ml; acidic FGF ED50 approximately equal to 6000 pg/ml) for many diverse cell types including capillary endothelial cells, vascular smooth muscle cells, and adrenocortical and granulosa cells; in vivo, basic FGF is a powerful angiogenic agent in the chick chorioallantoic membrane assay. The available protein sequence data demonstrate the existence of significant structural homology between the two polypeptides.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Cell Division / drug effects
  • Cells, Cultured
  • Cysteine / analysis
  • Fibroblast Growth Factors / analysis*
  • Fibroblast Growth Factors / isolation & purification
  • Fibroblast Growth Factors / pharmacology
  • Hydrogen-Ion Concentration
  • Mesoderm
  • Pituitary Gland / analysis*
  • Protein Conformation
  • Structure-Activity Relationship

Substances

  • Fibroblast Growth Factors
  • Cysteine