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
Hauptverfasser: Gospodarowicz, D., Cheng, J., Lui, G.-M., Fujii, D.K., Baird, A., Böhlen, P.
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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.
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(85)90082-8