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  Isolation of soy bean protein P34 from oil bodies using hydrophobic interaction chromatography

Sewekow, E., Keßler, L. C., Seidel-Morgenstern, A., & Rothkoetter, H.-J. (2008). Isolation of soy bean protein P34 from oil bodies using hydrophobic interaction chromatography. BMC Biotechnology, 8, 27. doi:10.1186/1472-6750-8-27.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0013-961A-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-8B38-1
Genre: Journal Article

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eDoc_339787_2008.pdf (Publisher version), 3MB
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This is an Open Access article distributed under the terms of the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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 Creators:
Sewekow, E.1, Author
Keßler, L. C.2, Author              
Seidel-Morgenstern, A.1, 2, Author              
Rothkoetter, H.-J.1, Author
Affiliations:
1Otto-von-Guericke-Universität Magdeburg, External Organizations, ou_1738156              
2Physical and Chemical Foundations of Process Engineering, Max Planck Institute for Dynamics of Complex Technical Systems, Max Planck Society, ou_1738150              

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 Abstract: Background Soybeans play a prominent role in allergologic research due to the high incidence of allergic reactions. For detailed studies on specific proteins it is necessary to have access to a large amount of pure substance. Results In this contribution, a method for purifying soybean (Glycine max) protein P34 (also called Gly m Bd 30K or Gly m 1) using hydrophobic interaction chromatography is presented. After screening experiments using 1 mL HiTrap columns, Butyl Sepharose 4 FF was selected for further systematic investigations. With this stationary phase, suitable operation conditions for two-step gradient elution using ammonium sulphate were determined experimentally. The separation conditions obtained in a small column could be scaled up successfully to column volumes of 7.5 and 75 mL, allowing for high product purities of almost 100% with a yield of 27 % for the chromatographic separation step. Conditions could be simplified further using a one-step gradient, which gave comparable purification in a shorter process time. The identity of the purified protein was verified using in-gel digestion and mass spectrometry as well as immunological techniques. Conclusions With the technique presented it is possible to produce, within a short timeframe, pure P34, suitable for further studies where an example antigen is needed. © 2008 Sewekow et al; licensee BioMed Central Ltd.

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Language(s): eng - English
 Dates: 2008
 Publication Status: Published in print
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 Rev. Type: -
 Identifiers: eDoc: 339787
DOI: 10.1186/1472-6750-8-27
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Title: BMC Biotechnology
Source Genre: Journal
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Publ. Info: BioMed Central
Pages: - Volume / Issue: 8 Sequence Number: - Start / End Page: 27 Identifier: ISSN: 1472-6750
CoNE: https://pure.mpg.de/cone/journals/resource/111000136906066