Skip to main content
U.S. flag

An official website of the United States government

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you’ve safely connected to the .gov website. Share sensitive information only on official, secure websites.

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.
No. 5


agarase and dextranase digestion, preparative separation, protein electrochromatography, whey proteins, Β-lactoglobulin


Tellez, C. and Cole, K. (2000), Preparative Electrochromatography of Proteins in Various Types of Porous Media, Electrophoresis (Accessed December 4, 2023)
Created February 29, 2000, Updated October 12, 2021