Amino-terminal sequences of a novel heparin-binding protein from human, bovine, rat, and chick brain: High interspecies homology

  title={Amino-terminal sequences of a novel heparin-binding protein from human, bovine, rat, and chick brain: High interspecies homology},
  author={Daniel Huber and P Gautschi-Sova and Peter Böhlen},
  journal={Neurochemical Research},
Recently, the partial structural characterization of a novel bovine brain protein was reported (1). Because of its mitogenic activity for vascular endothelial cells and its ability to strongly bind heparin it was termed heparin-binding brain mitogen (HBBM). Although HBBM shares these properties with members of the fibroblast growth factor (FGF) family of growth factors, its aminoterminal sequence is not homologous to that of the FGFs. Now, we report the isolation and partial structural… 
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    Proceedings of the National Academy of Sciences of the United States of America
  • 1985
The two major mitogenic polypeptides for endothelial cells have been purified to homogeneity and the available protein sequence data demonstrate the existence of significant structural homology between the two polyPEptides.
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