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Recent developments in the cell biology of basic fibroblast growth factor.

Recent developments in the cell biology of basic fibroblast growth factor. 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 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Cell Biology Rockefeller University Press

Recent developments in the cell biology of basic fibroblast growth factor.

The Journal of Cell Biology , Volume 109 (1): 1 – Jul 1, 1989

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References (71)

Publisher
Rockefeller University Press
Copyright
Copyright © 1989 by The Rockefeller University Press
ISSN
0021-9525
eISSN
1540-8140
DOI
10.1083/jcb.109.1.1
Publisher site
See Article on Publisher Site

Abstract

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

Journal

The Journal of Cell BiologyRockefeller University Press

Published: Jul 1, 1989

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