Caseinomacropeptide (CMP), aheterogeneous groupof peptides regarding the degree of glycosylation and phosphorylation, has so far not been effectively fractionated into its twomajor fractions: the glycosylated gCMP and the non-glycosylated aCMP. Therefore, an anion-exchange chromatography (AEC) process for the fractionation of CMP in those two fractions was developed and optimized. Furthermore, the method was applied to compare membrane adsorption chromatography (MAC) devices with classical bead-based column chromatography. It was shown that MAC devices can separate gCMP from aCMP, however, at a lower level of binding capacity and chromatographic resolution compared to classical chromatography. On the other hand, a fractionation is achieved at a four times faster separation speed.
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Caseinomacropeptide (CMP), aheterogeneous groupof peptides regarding the degree of glycosylation and phosphorylation, has so far not been effectively fractionated into its twomajor fractions: the glycosylated gCMP and the non-glycosylated aCMP. Therefore, an anion-exchange chromatography (AEC) process for the fractionation of CMP in those two fractions was developed and optimized. Furthermore, the method was applied to compare membrane adsorption chromatography (MAC) devices with classical bead-...
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