A heparin-binding erythroid cell stimulating factor from fetal bovine serum has the N-terminal sequence of insulin-like growth factor II
| Autor: | Qinggang Li, Frederick Esch, L. Fernando Congote, Russell Blacher |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
medicine.medical_specialty
medicine.medical_treatment Molecular Sequence Data Biophysics Fibroblast growth factor Biochemistry Chromatography Affinity Affinity chromatography Internal medicine medicine Animals Erythropoiesis Amino Acid Sequence Growth Substances Molecular Biology Interleukin 3 biology Heparin Growth factor Insulin Cell Biology Extracellular Matrix Endocrinology Insulin-like growth factor 2 biology.protein Cattle Apolipoprotein H Fetal bovine serum |
| Zdroj: | Biochemical and biophysical research communications. 166(2) |
| ISSN: | 0006-291X |
| Popis: | An 8 kd heparin-binding peptide which stimulates thymidine incorporation in cultures of fetal calf liver erythroid cells was isolated from fetal bovine serum by affinity chromatography on Heparin-Sepharose, ion exchange chromatography, gel filtration and reversed-phase HPLC. The N-terminal sequence of the isolated peptide was identical to the N-terminal sequence of bovine erythrotropin or insulin-like growth factor II (IGF II). The potential heparin-binding site of IGF II is probably situated in the arginine-rich C-peptide region. The affinities of human recombinant IGF I and II were compared with those of apolipoprotein H (a plasma heparin-binding protein) and bovine insulin in a heparin-affinity column. The retention times were in the order: Apolipoprotein H greater than hrIGF II greater than hrIGF I greater than insulin (no retention). This unusual property of IGF II suggests that it may be captured in the extracellular matrix in a similar way to fibroblast growth factor, interleukin 3 or granulocyte/macrophage colony-stimulating factor. |
| Databáze: | OpenAIRE |
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