Abstract
Recombinant human macrophage colony-stimulating factor (M-CSF), a disulfide-linked dimeric protein containing 18 cysteines, has been purified in monomeric form from E. coli and renatured to generate fully active dimers with an overall yield of 25 percent. M-CSF monomers were quantitatively refolded at concentrations as high as 0.7 mg/ml. Residual contaminants, including endotoxin, were removed from the refolded M-CSF by hydrophobic interaction chromatography. The kinetics of refolding and the characteristics of the renatured product were determined by measuring (1) molecular size, (2) biological activity, and (3) reactivity with a novel neutralizing monoclonal antibody specific for the dimeric form of M-CSF. The results show that refolded M-CSF from E. coli closely resembles both native and recombinant M-CSF produced by mammalian cells.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
