Purification, enzymatic activity and inhibitor discovery for recombinant human carbonic anhydrase XIV
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- 作者：Vaida Juozapaitienė ; vaida.jogaite@bti.vu.lt" class="auth_mail" title="E-mail the corresponding author ; jogaite@ibt.lt" class="auth_mail" title="E-mail the corresponding author ; Brigita Bartkutė ; Vilma Michailovienė ; Audrius Zak&scaron ; auskas ; Lina Baranauskienė ; Sandra Satkūnė ; Daumantas Matulis
- 关键词：Carbonic anhydrase XIV ; Recombinant protein expression ; E. coli ; Protein purification ; Protein activity ; Enzyme catalytic activity
- 刊名：Journal of Biotechnology
- 出版年：2016
- 出版时间：20 December 2016
- 年：2016
- 卷：240
- 期：Complete
- 页码：31-42
- 全文大小：1942 K
文摘
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Recombinant preparation of CA XIV, a difficult to produce protein, is described.
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Large amount of CA XIV was affinity purified using sulfonamide-modified sepharose.
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Inhibitor titration of activity demonstrated nearly 100% pure and active enzyme.
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Nanomolar inhibitors of CA XIV, selective over CA I and II, were designed.