Primary structure of ovine fibroblast growth factor-1 deduced by protein and cDNA analysis

Teri Wangler Grieb, Mary Ring, Ernest Brown, Carol Palmer, Natalie Belle, Dubravka Donjerkovic, Helena Chang, June Yun, Ramiah Subramanian, Farahnaz Forozan, Yan Guo, Akos Vertes, Jeffrey A. Winkles, Wilson H. Burgess

Research output: Contribution to journalArticlepeer-review


The amino acid sequence of full-length ovine fibroblast growth factor-1 (FGF-1) was determined by a combination of protein and cDNA sequencing. FGF-1 cDNA analysis indicated that ovine kidney cells express mRNAs encoding both full length FGF-1 and a truncated FGF-1 variant. An overall comparison of the ovine FGF-1 primary sequence to the eight species studied to date revealed a high degree of conservation, with ovine FGF-1 sharing 90 and 95% sequence identity with human FGF-1 and bovine FGF-1, respectively. Additionally, the FGF-1 proteins from the various species have conserved cysteine residues at positions 30 and 97 and contain acetylated amino-terminal alanine residues. Mass spectrometry analysis confirmed that the blocking group of ovine FGF-1 is also consistent with that of an acetyl-moiety. In contrast to the other FGF-1 proteins, the 154 residue primary sequence of ovine FGF-1 contains three unique amino acid differences: Arg9, Arg44, and Ile123. Ovine FGF-1, unlike human FGF-1, is a potent mitogenic factor for NIH 3T3 fibroblasts in the absence of heparin. In the presence of exogenous heparin, the mitogenic activity of ovine FGF-1 is potentiated slightly.

Original languageEnglish (US)
Pages (from-to)182-191
Number of pages10
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - May 8 1998
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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