Purification and partial characterization of bovine pituitary fibroblast growth factor

Sandra K. Lemmon, Ralph A. Bradshaw

Research output: Contribution to journalArticle

22 Scopus citations

Abstract

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 ∼20‐fold, was achieved by electro‐phoresis in polyacrylamide gels at acid pH. The mitogenic peptide has a molecular weight of 14,500–15,00 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.

Original languageEnglish (US)
Pages (from-to)195-208
Number of pages14
JournalJournal of cellular biochemistry
Volume21
Issue number3
DOIs
StatePublished - 1983
Externally publishedYes

Keywords

  • amino acid analysis
  • pituitary fibroblast growth factor
  • silver staining

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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