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

J Cell Physiol. 1985 Feb;122(2):323-32. doi: 10.1002/jcp.1041220223.

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.

MeSH terms

  • Animals
  • Aorta, Thoracic / cytology
  • Aorta, Thoracic / drug effects
  • Cattle
  • Cell Division / drug effects
  • Cells, Cultured
  • Chemical Phenomena
  • Chemistry
  • Chromatography / methods
  • Drug Stability
  • Endothelium / cytology
  • Endothelium / drug effects
  • Fibroblast Growth Factors / isolation & purification*
  • Fibroblast Growth Factors / pharmacology
  • Pituitary Gland / analysis*

Substances

  • Fibroblast Growth Factors