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N the past four years there has been an enormous increase in research involving basic fibroblast growth factor (FGF) t as a result of the development of effective methods for the isolation of the protein and the availability of characterized nucleic acid probes, specific antibodies, and recombinant growth factor. Several reviews have been published describing much of the basic biology of acidic FGF (aFGF) and basic FGF (bFGF) (5, 25, 33). Therefore, in this mini-review we have focused on specific areas in bFGF biology in which uncertainties exist. For simplicity, we have confined this review to bFGF. However, some of the questions concerning bFGF also apply to aFGF and are discussed. History FGF was originally identified as an activity in extracts of pituitary and brain that stimulated the growth of 3T3 cells (3, 23). The activity was shown to be due to two proteins. One of them, aFGF, had an acidic pI (5.6) and eluted from heparin-Sepharose with I M NaC1 (34, 65). The second, bFGF, had a basic pI (>9.0), eluted from heparin-Sepharose at 1.5 M NaCI, and had 55 % sequence homology to aFGF (14). The introduction of heparin-affinity chromatography facilitated the isolation of sufficient quantities
The Journal of Cell Biology – Rockefeller University Press
Published: Jul 1, 1989
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