Abstract
Recombinant human acidic fibroblast growth factor has been produced in E. coli cells at a level of at least 50 mg/l culture. The recombinant and natural acidic fibroblast growth factors are almost identical to one another when tested on rat mammary fibroblasts for their ability to stimulate DNA synthesis, to bind to the high-affinity surface receptors of the cells and to inhibit DNA synthesis when present in the culture medium at high concentrations. The recombinant acidic fibroblast growth factor binds to two cell-surface polypeptides of molecular masses 160 kDa and 140 kDa, which are the same size as the receptors for basic fibroblast growth factor, and it binds preferentially to the smaller polypeptide.
| Original language | English |
|---|---|
| Pages (from-to) | 963-971 |
| Number of pages | 9 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 171 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 28 Sept 1990 |
| Externally published | Yes |