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. 1998 Dec 18;828(1-2):365-72.
doi: 10.1016/s0021-9673(98)00521-4.

Protein variant separations by cation-exchange chromatography on tentacle-type polymeric stationary phases

M Weitzhandler  1 , D Farnan, J Horvath, J S Rohrer, R W Slingsby, N Avdalovic, C Pohl
Affiliations

Protein variant separations by cation-exchange chromatography on tentacle-type polymeric stationary phases

M Weitzhandler et al. J Chromatogr A. .

Abstract

We developed a set of prototype cation-exchange column packings that are based on a hydrophilic coated, pellicular polymeric support with a grafted tentacular surface chemistry that is highly suited to resolving closely related protein variants. These column packings (1) afford minimal band spreading in conjunction with extremely high selectivity, (2) exhibit a very hydrophilic character and (3) have moderate loading capacity. Cytochrome c variants (bovine, horse, rabbit) were baseline-separated, as was native ribonuclease A and its two deamidation products, the Asp67 and isoAsp67 forms. Humanized monoclonal antibody variants differing in the presence of lysine at the C terminus of the heavy chains were baseline-resolved. Finally, the separation of hemoglobin variants found in a sample containing elevated levels of glycated hemoglobin was also demonstrated.

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