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Copyrights © 2008 , Sevas Educational Society, All rights Reserved |
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Mapping the chromatographic behavior of a cell proteome utilizing orthogonal routines: the influence of feedstock pH |
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More Articles
Special Contributions
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Rosa Cabrera and Marcelo Fernandez-Lahore * |
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Downstream Processing Laboratory. School of Engineering and Science. Jacobs University gGmbH. Campus Ring 1, D-28759, Bremen, Germany |
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Received: 3 August 2008 / Received in revised form: 15 August 2008, Accepted: 19 August 2008, Published online: 20 August 2008 |
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Abstract |
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Surface charge, molecular weight, and folding state are known to influence protein chromatographic behavior onto ion-exchangers. Experimentally, information related to such factors can be gathered via two-dimensional electrophoretic (2-DE) methods. |
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The separation behavior depicted by the insect cultured-cells proteome, which is an important host for recombinant protein production, was explored in this study. Experimental evidence showed a correlation between apparent isoelectric point distributions and the mobile phase conductivity. It was observed that the information contained in the isoelectric point (pI) value(s) obtained with a 2-DE routine showed a good correlation with the IEX chromatographic behavior, for a number of commercial adsorbents. This correlation was observed irrespective of the pH of the feedstock within the range 6 to 8. An initial prediction of protein ion-exchange chromatographic behavior could be possible utilizing an experimental approach based on the mentioned orthogonal methods. This technique is providing information that more closely resembles the separation behaviour observed with a complex biotechnological feedstock. |
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Keywords: Insect cells, proteome, chromatography, ion-exchange,
bioprocessing |
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*Tel: 00494212003172, Fax: 00494212003660 |
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| Volume 1, Issue 1, August 2008, Page No. 01-05 |
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