Chromatography on DEAE ion-exchange and Protein G affinity columns in tandem for the separation and purification of proteins.
A high-performance liquid-chromatographic method based on coupled DEAE anion-exchange and Protein G affinity columns has been developed for the simultaneous separation and purification of immunoglobulin G and albumin from mouse serum. The diluted mouse serum was injected directly into this system, and the proteins were eluted separately from the DEAE and Protein G columns, coupled in series, by the column-switching technique. The advantages of this method are that IgG and albumin can be separated and purified simultaneously, the expensive affinity column is protected from contamination by the impurities in the mouse serum, and it is fast, selective, robust, and reproducible.
Qi
Y
Y
Research Center for Eco-Environmental Sciences, Chinese Academy of Sciences, PO Box 2871, Beijing 100085, China.
Yan
Z
Z
Huang
J
J
D000818:Animals; D002846:Chromatography, Affinity / Q000295:instrumentation / Q000379:methods*; D002848:Chromatography, DEAE-Cellulose / Q000379:methods*; D004867:Equipment Design; D007074:Immunoglobulin G / Q000097:blood* / Q000302:isolation & purification; D007202:Indicators and Reagents; D051379:Mice; D009419:Nerve Tissue Proteins; D011506:Proteins / Q000302:isolation & purification*; D012680:Sensitivity and Specificity; D012709:Serum Albumin / Q000302:isolation & purification*
C029152:G-substrate; D007074:Immunoglobulin G; D007202:Indicators and Reagents; D009419:Nerve Tissue Proteins; D011506:Proteins; D012709:Serum Albumin