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Purification of transferrin from Cohn supernatant I using ion‐exchange chromatography
Author(s) -
McCann Karl B.,
Hughes Ben,
Wu John,
Bertolini Joseph,
Gomme Peter T.
Publication year - 2005
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1042/ba20050065
Subject(s) - transferrin , chromatography , ion chromatography , chemistry , ion exchange , albumin , sepharose , column chromatography , affinity chromatography , biochemistry , ion , enzyme , organic chemistry
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.