Literature DB >> 9914658

Comparison of loading capacities of various proteins and peptides in culture medium and in pure state.

A Staby1, N Johansen, H Wahlstrøm, I Mollerup.   

Abstract

Chromatographic media suppliers most frequently state the capacities of their gels based on either static capacities or frontal analysis experiments of pure proteins, however, these capacity values are often far from the capacities experienced in the production of such proteins. In this work static and dynamic capacities of various pure industrial proteins or peptides are compared to the capacities of the proteins or peptides under similar conditions in their natural culture medium. The results show a significant decrease in the static and dynamic capacities of the proteins or peptides when present in culture medium due to competitive binding of medium proteins. The proteins and peptides included in this study are: lipolase, glucagon-like peptide-1, truncated prothrombin, insulin precursor, and anti-Factor VII monoclonal antibody.

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Year:  1998        PMID: 9914658     DOI: 10.1016/s0021-9673(98)00764-x

Source DB:  PubMed          Journal:  J Chromatogr A        ISSN: 0021-9673            Impact factor:   4.759


  1 in total

1.  Fouling of an anion exchange chromatography operation in a monoclonal antibody process: Visualization and kinetic studies.

Authors:  Edward J Close; Jeffrey R Salm; Timothy Iskra; Eva Sørensen; Daniel G Bracewell
Journal:  Biotechnol Bioeng       Date:  2013-03-31       Impact factor: 4.530

  1 in total

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