Isolation, renaturation and partial characterization of recombinant human transferrin and its half molecules from escherichia coli

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-...

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Bibliographic Details
Published in:The international journal of biochemistry & cell biology 1996-09, Vol.28 (9), p.975-982
Main Authors: Hoefkens, Peter, De Smit, Maarten H., De Jeu-Jaspars, Nel M.H., Huijskes-Heins, Marja I.E., De Jong, Gerard, Van Eijk, Hendrik G.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Electron Spin Resonance Spectroscopy
Electrophoresis, Polyacrylamide Gel
Escherichia coli
Humans
Inclusion bodies
Iron
Molecular Sequence Data
Recombinant Proteins - chemistry
Recombinant Proteins - isolation & purification
Recombinant transferrin
Renaturation
Transferrin - chemistry
Transferrin - isolation & purification
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Summary: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.
ISSN:1357-2725
1878-5875
DOI:10.1016/1357-2725(96)00057-X