| Autor: |
Hoefkens P; Department of Chemical Pathology, Erasmus University, Rotterdam, The Netherlands., de Smit MH, de Jeu-Jaspars NM, Huijskes-Heins MI, de Jong G, van Eijk HG |
| Jazyk: |
angličtina |
| Zdroj: |
The international journal of biochemistry & cell biology [Int J Biochem Cell Biol] 1996 Sep; Vol. 28 (9), pp. 975-82. |
| DOI: |
10.1016/1357-2725(96)00057-x |
| Abstrakt: |
Recombinant human transferrin as well as N- and C-terminal half-transferrins, produced in Escherichia coli, are deposited in inclusion bodies by the bacteria. The isolation and purification of the recombinant proteins from these inclusion bodies are described here. The amino acid compositions and N-terminal sequences of the proteins were determined, and found to be in agreement with the known protein structure of human serum transferrin. Renaturation of the recombinant proteins is described, resulting in water-soluble iron-binding molecules. Iron binding was confirmed by 59Fe labelling, absorption spectrophotometry and EPR spectrometry. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
|
Full Text from ScienceDirect