Purification of transferrin from Cohn supernatant I using ion-exchange chromatography.
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.
McCann
Karl B
KB
Research and Development Department, CSL Bioplasma, 189-209 Camp Rd, Broadmeadows, VIC 3047, Australia.
Hughes
Ben
B
Wu
John
J
Bertolini
Joseph
J
Gomme
Peter T
PT
D005591:Chemical Fractionation; D002848:Chromatography, DEAE-Cellulose; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D005240:Feasibility Studies; D006801:Humans; D007074:Immunoglobulin G / Q000302:isolation & purification; D012709:Serum Albumin / Q000302:isolation & purification; D014168:Transferrin / Q000302:isolation & purification*
D007074:Immunoglobulin G; D012709:Serum Albumin; D014168:Transferrin