ISSN:
1573-6903
Keywords:
Heparin-binding protein
;
N-terminal sequence
;
sequence homology
;
brain
;
human
;
bovine
;
rat
;
chicken
Source:
Springer Online Journal Archives 1860-2000
Topics:
Medicine
Notes:
Abstract 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 characterization of HBBMs from human, rat and chick brain. Proteins were isolated by tissue extraction at pH 4.5, ammonium sulfate precipitation, cation exchange chromatography, heparin-Sepharose affinity chromatography and reverse-phase HPLC. The amino-terminal sequences of the HBBMs from human, bovine and rat brain are identical, whereas that of chick HBBM reveals a single amino acid substitution. The high sequence homology among the HBBMs from different species suggests an important biological role of the protein.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00969930
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