Advanced purification strategy for CueR, a cysteine containing copper(I) and DNA binding protein
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- 作者：Ria K. Balogha ; Bé ; la Gyurcsika ; É ; va Hunyadi-Gulyá ; sb ; Hans E.M. Christensenc ; hemc@kemi.dtu.dk" class="auth_mail" title="E-mail the corresponding author ; Attila Jancsó ; a ; jancso@chem.u-szeged.hu" class="auth_mail" title="E-mail the corresponding author
- 关键词：Metalloregulatory proteins ; Cysteine ; Copper(I) ; DNA binding ; Four step purification
- 刊名：Protein Expression and Purification
- 出版年：2016
- 出版时间：July 2016
- 年：2016
- 卷：123
- 期：Complete
- 页码：90-96
- 全文大小：1301 K
文摘
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Bacterial transcription factor CueR was expressed and purified.
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DNA content of the lysed cells were removed by enzymatic digestion.
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The four step chromatographic procedure yielded the pure metalloregulatory protein.
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CD spectrum of CueR is characteristic for proteins with high α-helical content.
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Functionality of the purified protein was proven by gel mobility shift assay.