The present paper describes an anion-exchange chromatography method to separate iron-free apo-Tf (apo-transferrin) from albumin and IgG in Cohn supernatant I. The method uses DEAE-fast flow Sepharose chromatography along with optimized protein concentration (5%, w/v) and column operation conditions (40 g/l, conductivity < 1.0 mS/cm) to resolve apo-Tf from IgG and albumin. The single step purifies apo-Tf to > 90% and provides an efficient means to obtain commercial quantities of the protein.
ASJC Scopus subject areas
- Molecular Medicine
- Biomedical Engineering
- Applied Microbiology and Biotechnology
- Drug Discovery
- Process Chemistry and Technology
McCann, K. B., Hughes, B., Wu, J., Bertolini, J., & Gomme, P. T. (2005). Purification of transferrin from Cohn supernatant I using ion-exchange chromatography. Biotechnology and Applied Biochemistry, 42(3), 211-217. https://doi.org/10.1042/BA20050065