University of Natural Resources and Life Sciences, Vienna (BOKU) - Research portal
Selected Publication:
Ueberbacher, R; Haimer, E; Hahn, R; Jungbauer, A.
(2008):
Hydrophobic interaction chromatography of proteins V. Quantitative assessment of conformational changes.
J Chromatogr A. 2008; 1198-1199:154-163
FullText
FullText_BOKU
- Abstract:
- Protein adsorption during hydrophobic interaction chromatography (HIC) may induce conformational changes. We analyzed conformational changes in three model proteins, bovine serum albumin (BSA), P-lactoglobulin, and lysozyme by attenuated total reflectance Fourier transform infrared (ATR FF-IR) spectroscopy and pulse response experiments. Conformational changes occurred in the secondary structure of BSA, the tertiary structure of P-lactoglobulin, and no changes occurred in lysozyme under the adsorption conditions investigated. Protein unfolding varied substantially among proteins, caused incomplete isocratic elution in HIC, and was confirmed by in situ assessments. Lower temperatures and binding capacities significantly reduced protein unfolding; the activation energy for unfolding ranged from 47 to 125 kJ/mol. (c) 2008 Elsevier B.V. All rights reserved.
- Authors BOKU Wien:
- Hahn Rainer
- Haimer Emmerich
- Jungbauer Alois
- Find related publications in this database (using NML MeSH Indexing)
- Adsorption -
- Animals -
- Cattle -
- Chromatography - methods
- Hydrophobicity -
- Lactoglobulins - chemistry
- Muramidase - chemistry
- Protein Conformation -
- Proteins - chemistry
- Reproducibility of Results -
- Serum Albumin, Bovine - chemistry
- Spectroscopy, Fourier Transform Infrared -
- Temperature -
- Find related publications in this database (Keywords)
- hydrophobic interaction chromatography
- adsorption
- attenuated total reflectance Fourier transform infrared spectroscopy
- protein stability
- conformational changes
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