Purification of basic fibroblast growth factor from rat brain: identification of a Mr 22,000 immunoreactive form.
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.
Presta
M
M
Dept. Biomedical Sciences and Biotecnology, School of Medicine, University of Brescia, Italy.
Rusnati
M
M
Maier
J A
JA
Ragnotti
G
G
D000818:Animals; D001923:Brain Chemistry; D002417:Cattle; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D004305:Dose-Response Relationship, Drug; D004727:Endothelium / Q000187:drug effects / Q000378:metabolism; D005346:Fibroblast Growth Factors / Q000302:isolation & purification*; D008970:Molecular Weight; D010960:Plasminogen Activators / Q000378:metabolism
D005346:Fibroblast Growth Factors; D010960:Plasminogen Activators