Purification of basic fibroblast growth factor from rat brain: identification of a Mr 22,000 immunoreactive form.
Articolo
Data di Pubblicazione:
1988
Abstract:
A 18,000-dalton protein which stimulates plasminogen activator (PA) activity in endothelial GM 7373 cells has been purified from rat brain by using heparin affinity chromatography and ion-exchange chromatography. The purified molecule stimulates PA activity in a dose-dependent manner between 1 and 30 ng/ml. It also stimulates proliferation of GM 7373 cells and DNA synthesis in NIH 3T3 cells in a similar concentration range. The molecule has been identified as a bFGF-like molecule on the basis of its biological activity, its affinity for heparin-Sepharose, and its cross-reactivity with anti-human bFGF antibodies. In the final preparation of the rat brain bFGF, trace amounts (less than 5\%) of a contaminant were detectable. This contaminant has a molecular weight of 22,000 and cross reacts with several anti-human placental bFGF antibodies. On the basis of its affinity for heparin-Sepharose and its immunological characteristics, this protein appears to be an high molecular weight form of bFGF.
Tipologia CRIS:
1.1 Articolo in rivista
Keywords:
Animals; Brain Chemistry; Cattle; Chromatography; Affinity; Ion Exchange; Dose-Response Relationship; Drug; Endothelium; Fibroblast Growth Factors; Molecular Weight; Plasminogen Activators
Elenco autori:
Presta, Marco; Rusnati, Marco; J. A., Maier; G., Ragnotti
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