Preparative Electrochromatography of Proteins in Various Types of Porous Media
C M. Tellez, Kenneth D. Cole
The performance of commercial and enzymatically-modified size-exclusion (SE) gels in electrochromatography was compared for preparative protein separations. Dextran and agarose-based SE gels were subjected to enzymatic digestion under mild conditions. This treatment partially hydrolyzed the gel matrix modifying its pore-size distribution. Enzymatic treatment of agarose-based SE gels was found to increase the resolution of the separation. Successful separation of preparative amounts of the A and B forms of β-lactoglobulin (difference in electrophoretic mobility of 8.5 %) was achieved with a high degree of purity using agarose-based SE gels. The four major whey proteins, β-lactoglobulin, α-lactalbumin, BSA and immunoglobulins, were purified from an acid whey preparation. The degree of retention of a protein in electrochromatography followed their free-solution electrophoretic mobility ( ) when the protein was able to enter the gel pores and the ratio of diffusion/ when the protein was excluded.
agarase and dextranase digestion, preparative separation, protein electrochromatography, whey proteins, Β-lactoglobulin
and Cole, K.
Preparative Electrochromatography of Proteins in Various Types of Porous Media, Electrophoresis
(Accessed December 4, 2023)