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Purification of transferrin from Cohn supernatant I using ion-exchange chromatography
Karl B McCann1, Ben Hughes, John Wu
1Research and Development Department, CSL Bioplasma, 189-209 Camp Rd, Broadmeadows, VIC 3047, Australia.
Abstract:
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.
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