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Effects of protein conformational changes on separation performance in electrostatic interaction chromatography: Unfolded proteins and PEGylated proteins

Paper ID Volume ID Publish Year Pages File Format Full-Text
24948 43547 2007 6 PDF Available
Title
Effects of protein conformational changes on separation performance in electrostatic interaction chromatography: Unfolded proteins and PEGylated proteins
Abstract

As it is important to understand how protein conformational changes affect the separation performance in ion exchange chromatography (IEC), we investigated two model systems, unfolded proteins (lysozyme and bovine serum albumin) with urea and dithiothreitol, and PEGylated proteins (lysozyme attached with polyethyleneglycol molecular weight 5000). Linear gradient elution IEC experiments were carried out and the data were analysed by our model previously presented in order to obtain the binding site value B and the peak salt concentration IR. Unfolded proteins (bovine serum albumin and lysozyme) with urea and dithiothreitol showed weaker retention and larger binding site values compared with the values for native proteins. Multiple PEGylated lysozyme peaks were separated, and eluted earlier than the native peak appeared. There is a good correlation between B and IR for PEGylated lysozymes.

Keywords
Ion exchange chromatography; Unfolded proteins; PEGylated proteins; Retention; Binding site
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Effects of protein conformational changes on separation performance in electrostatic interaction chromatography: Unfolded proteins and PEGylated proteins
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 132, Issue 2, 31 October 2007, Pages 196–201
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us