| abstract |
A method for producing a naturally folded eukaryotic polypeptide, containing two or more cysteines linked via disulfide bridges, by a) culturing prokaryotic cells, the prokaryotic cells mentioned containing an expression vector which, for the polypeptide mentioned, contains a prokaryotic signal sequence at the N-terminus , coded, b) secretion of the polypeptide into the periplasm or the medium, c) cleavage of the signal sequence and isolation of the polypeptide from the periplasm or the medium, characterized in that in the said prokaryotic cell, a nucleic acid coding for a molecular chaperone is additionally expressed and the chaperone is secreted into the periplasm, is suitable for the recombinant production of polypeptides in prokaryotes with high yield. |