Purification of recombinant ovalbumin from inclusion bodies of Escherichia coli
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- 作者：Vaibhav Upadhyay ; Anupam Singh ; Amulya K. Panda ; amulya@nii.res.in" class="auth_mail" title="E-mail the corresponding author
- 关键词：E. coli ; Escherichia coli ; ova ; ovalbumin ; SDS ; sodium dodecyl sulfate ; PAGE ; polyacrylamide gel electrophoresis ; CD ; circular dichroism ; LB ; Luria Bertani ; IPTG ; isopropyl β-d-thio galactopyranoside ; HPLC ; high performance liquid chromatography ; IBs ; inclusion bodies ; GdnHCl ; guanidine hydrochloride ; ESI-MS ; electrospray ionization mass spectrometry ; DEAE ; Diethylaminoethanol
- 刊名：Protein Expression and Purification
- 出版年：2016
- 出版时间：January 2016
- 年：2016
- 卷：117
- 期：Complete
- 页码：52-58
- 全文大小：1614 K
文摘
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Ovalbumin was expressed in E. coli without any posttranslational modification.
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Most of the recombinant ovalbumin was expressed as inclusion bodies.
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Solubilization using urea followed by dilution resulted in refolded ovalbumin.
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Recombinant refolded ovalbumin has similar biophysical characteristics to that of native ovalbumin.