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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Denoroy, L. Esch, F. Guillemin, R. Ling, N. Hill, F. Ueno, N. Böhlen, P. Klepper, R. Gospodarowicz, D. Baird, A. |
| Abstract | The two major mitogenic polypeptides for endothelial cells have been purified to homogeneity. The complete primary structure of bovine pituitary basic fibroblast growth factor (FGF) and the amino-terminal amino acid sequence of bovine brain acidic FGF have been established by gas-phase sequence analyses. Homogeneous preparations of these polypeptides are potent mitogens (basic FGF, ED50 approximately equal to 60 pg/ml; acidic FGF ED50 approximately equal to 6000 pg/ml) for many diverse cell types including capillary endothelial cells, vascular smooth muscle cells, and adrenocortical and granulosa cells; in vivo, basic FGF is a powerful angiogenic agent in the chick chorioallantoic membrane assay. The available protein sequence data demonstrate the existence of significant structural homology between the two polypeptides. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 19 |
| Volume Number | 82 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1985-10-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Fibroblast Growth Factors Pituitary Gland Amino Acid Sequence Animals Cell Division Drug Effects Cells, Cultured Cysteine Isolation & Purification Pharmacology Hydrogen-Ion Concentration Mesoderm Protein Conformation Structure-Activity Relationship Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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