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-transf errins, produced in Escherichia coli, are deposited in inclusion bodie s by the bacteria. The isolation and purification of the recombinant p roteins from these inclusion bodies are described here. The amino acid compositions acid N-terminal sequences of the proteins were determine d, and found to be in agreement with the known protein structure of hu man serum transferrin. Renaturation of the recombinant proteins is des cribed, resulting in water-soluble iron-binding molecules. Iron bindin g was confirmed by Fe-59 labelling, absorption spectrophotometry and E PR spectrometry. Copyright (C) 1996 Elsevier Science Ltd