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Purification and partial characterization of bovine pituitary fibroblast growth factor

✍ Scribed by Sandra K. Lemmon; Ralph A. Bradshaw

Publisher
John Wiley and Sons
Year
1983
Tongue
English
Weight
770 KB
Volume
21
Category
Article
ISSN
0730-2312

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✦ Synopsis

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 ^3^H‐thymidine in Balb/c 3T3 cells. A preliminary amino acid composition is presented.

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