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

Abstract：

: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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Grieb TW,Ring M,Brown E,Palmer C,Belle N,Donjerkovic D,Chang H,Yun J,Subramanian R,Forozan F,Guo Y,Vertes A,Winkles JA,Burgess WH

doi

10.1006/bbrc.1998.8597

subject

Has Abstract

pub_date

1998-05-08 00:00:00

pages

182-91

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(98)98597-7

journal_volume

246

pub_type

杂志文章

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