Investigation of particle-based and monolithic columns for cation exchange protein displacement chromatography using poly(diallyl-dimethylammonium chloride) as displacer

Title data

Schmidt, Beata ; Wandrey, Christine ; Freitag, Ruth:
Investigation of particle-based and monolithic columns for cation exchange protein displacement chromatography using poly(diallyl-dimethylammonium chloride) as displacer.
In: Journal of Chromatography A. Vol. 1018 (2003) Issue 2 . - pp. 155-167.
ISSN 0021-9673
DOI: https://doi.org/10.1016/S0021-9673(03)01326-8

Official URL:

Abstract in another language

The overall topic of the investigation was the separation of basic proteins by cation exchange displacement chromatography. For this purpose two principal column morphologies were compared for the separation of ribonuclease A and α-chymotrypsinogen, two proteins found in the bovine pancreas. These were a column packed with porous particles (Macro-Prep S, 10 μm, 1000 Å) and a monolithic column (UNO™ S1). Both columns are strong cation exchangers, carrying SO3−-groups linked to a hydrophilic polymer support. Poly(diallyl-dimethylammonium chloride) (PDADMAC), a linear cationic polyelectrolyte composed of 100–200 quaternary pyrrolidinium rings, was used as displacer. The steric mass action (SMA) model and, in particular, the operating regime and dynamic affinity plots were used to aid method development. To date the {SMA} model has been applied primarily to simulate non-linear displacement chromatography of proteins using low molar mass displacers. Here, the model is applied to polyelectrolytes with a molar mass below 20 000 g mol−1, which corresponds to a degree of polymerization below 125 and an average contour length of less than 60 nm. The columns were characterized in terms of the adsorption isotherms (affinity, capacity) of the investigated proteins and the displacer.

Further data

Item Type:	Article in a journal
Refereed:	Yes
Keywords:	Proteins
Institutions of the University:	Faculties > Faculty of Engineering Science > Chair Process Biotechnology > Chair Process Biotechnology - Univ.-Prof. Dr. Ruth Freitag Faculties Faculties > Faculty of Engineering Science Faculties > Faculty of Engineering Science > Chair Process Biotechnology
Result of work at the UBT:	No
DDC Subjects:	500 Science 500 Science > 500 Natural sciences 600 Technology, medicine, applied sciences 600 Technology, medicine, applied sciences > 620 Engineering
Date Deposited:	25 Feb 2016 14:50
Last Modified:	30 Jun 2022 09:37
URI:	https://eref.uni-bayreuth.de/id/eprint/31061