Purification and partial characterization of bovine pituitary fibroblast growth factor

Purification and partial characterization of bovine pituitary fibroblast growth factor A purification procedure and partial characterization of bovine pituitary fibroblast growth factor (FGF) are described. The steps of the published methods [3,4] which yield inhomogeneous material, were retained, with modifications. The final isolation, with an additional purification of ∼20‐fold, was achieved by electro‐phoresis in polyacrylamide gels at acid pH. The mitogenic peptide has a molecular weight of 14,500–15,00 as determined on SDS gels, chromatographs as a monomer in nondenaturing conditions, and is active at the picomolar level in effecting the incorporation of 3H‐thymidine in Balb/c 3T3 cells. A preliminary amino acid composition is presented. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Cellular Biochemistry Wiley

Purification and partial characterization of bovine pituitary fibroblast growth factor

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Publisher
Wiley
Copyright
Copyright © 1983 Wiley Subscription Services
ISSN
0730-2312
eISSN
1097-4644
D.O.I.
10.1002/jcb.240210302
Publisher site
See Article on Publisher Site

Abstract

A purification procedure and partial characterization of bovine pituitary fibroblast growth factor (FGF) are described. The steps of the published methods [3,4] which yield inhomogeneous material, were retained, with modifications. The final isolation, with an additional purification of ∼20‐fold, was achieved by electro‐phoresis in polyacrylamide gels at acid pH. The mitogenic peptide has a molecular weight of 14,500–15,00 as determined on SDS gels, chromatographs as a monomer in nondenaturing conditions, and is active at the picomolar level in effecting the incorporation of 3H‐thymidine in Balb/c 3T3 cells. A preliminary amino acid composition is presented.

Journal

Journal of Cellular BiochemistryWiley

Published: Jan 1, 1983

Keywords: ; ;

References

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