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Cited by 492

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Purification of the fibroblast growth factor activity from bovine brain.

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Gospodarowicz, D., Bialecki, H., Greenburg, G.·1978·Journal of Biological Chemistry

Abstract

The purification of the fibroblast growth factor (FGF) from bovine brain has led to the isolation of two peptides. FGF-1 with 128 amino acids and FGF-2 with 107 amino acids. The biological activity of these two peptides is acid- and heat-labile. As indicated by the amino acid composition of FGF-1 and -2, these two peptides are derived from a common precursor and bear no resemblance to pituitary FGF. The brain FGF peptides, like pituitary FGF, are mitogenic in vitro for the same wide variety of mesoderm-derived cells. Since their mitogenic activity is acid- and heat-labile, they are thereby distinguished from the platelet factor isolated from platelets and from the cationic peptide isolated from serum which has been shown to have the same molecular weight and isoelectric point as brain and pituitary FGF.

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Metadata

Authors
Gospodarowicz, D., Bialecki, H., & Greenburg, G.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1978-05
Volume
253
Issue
10
Pages
3736-3743
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1502488284
Cited by
492
References
0
FWCI
12.90
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Purification of the fibroblast growth factor activity from bovine brain. https://app.cochat.ai/papers/10.1016/s0021-9258(17)34863-9
The paper
Gospodarowicz, D., Bialecki, H., & Greenburg, G. (1978). Purification of the fibroblast growth factor activity from bovine brain. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)34863-9

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.