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Protein Methodology¹

Chromatography of Milk Proteins on DEAE Cellulose^,2

Department of Food Science and Technology, University of California, Davis

ABSTRACT

The common organic ion exchange resins suitable for smaller molecules have been in use for over 20 yr, but these types of ion exchangers were found not suitable for chromatographic fractionation of proteins. As Sober and Peterson (7) have pointed out, the limitation of resins is their irreversible binding of many proteins, the results of the formation of too many bonds between protein molecules and the adsorbent. In such cases, the protein is so tightly bound to the adsorbent that the elution can be accomplished only under conditions destructive to the native configuration of protein.

This limitation of ion exchange resins led Peterson and Sober (3) in 1956 to develop a different type of adsorbent for chromatography of proteins—cellulosic ion exchangers. In the last 5 yr significant and rapid progress has been made in the synthesis of anionic and cationic cellulose exchangers, the methodology of fractionation, and the demonstration of the usefulness of these adsorbents, especially for separation of proteins when it is essential to preserve enzymatic or other biological activity.

¹ Presented at the A.D.S.A. Annual Meeting, University of Wisconsin, June 14, 1961.

² This study was supported in part by funds from the California Dairy Industry Advisory Board.

³ References for specific applications of these cellulose ion exchangers are numerous and can be obtained from BIO-RAD Laboratories, Richmond, California.