Fibroblast growth factor in the human placenta
Fibroblast growth factor (FGF) has been purified 333,000-fold from human placenta by a combination of salt precipitation, cation-exchange chromatography, and Heparin-Sepharose affinity chromatography. Molecular weight (15–16 kDaltons), amino acid composition, bioactivity and immunological crossreact...
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Veröffentlicht in: | Biochemical and biophysical research communications 1985-04, Vol.128 (2), p.554-562 |
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Hauptverfasser: | , , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Fibroblast growth factor (FGF) has been purified 333,000-fold from human placenta by a combination of salt precipitation, cation-exchange chromatography, and Heparin-Sepharose affinity chromatography. Molecular weight (15–16 kDaltons), amino acid composition, bioactivity and immunological crossreactivity with bovine pituitary FGF indicate that the mitogens from the two species are closely related molecules. |
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ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1016/0006-291X(85)90082-8 |