| Autor: |
de Smit MH; Leiden Institute of Chemistry, Department of Biochemistry, Gorlaeus Laboratories, Leiden University, The Netherlands., Hoefkens P, de Jong G, van Duin J, van Knippenberg PH, van Eijk HG |
| Jazyk: |
angličtina |
| Zdroj: |
The international journal of biochemistry & cell biology [Int J Biochem Cell Biol] 1995 Aug; Vol. 27 (8), pp. 839-50. |
| DOI: |
10.1016/1357-2725(95)00040-v |
| Abstrakt: |
Transferrin is a glycoprotein functioning in iron transport in higher eukaryotes, and consists of two highly homologous domains. To study the function of the glycan residues attached exclusively to the C-terminal domain, we have constructed a plasmid allowing production of nonglycosylated human transferrin in Escherichia coli. By molecular biological and genetic techniques, production was stepped up to 60 mg/l. Similar plasmids were constructed for production of the two half-transferrins. The recombinant proteins accumulate in inclusion-body-like aggregates, where they appear to bind iron without causing bacteriostasis. Proteins active in iron binding have been purified from these inclusion bodies. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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