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An efficient method to purify active eukaryotic proteins from the inclusion bodies in Escherichia coli.

作者信息

Lin K H, Cheng S Y

机构信息

Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.

出版信息

Biotechniques. 1991 Dec;11(6):748, 750, 752-3.

PMID:1809329
Abstract
摘要

相似文献

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An efficient method to purify active eukaryotic proteins from the inclusion bodies in Escherichia coli.一种从大肠杆菌包涵体中纯化活性真核蛋白的有效方法。
Biotechniques. 1991 Dec;11(6):748, 750, 752-3.
2
Solubilization of Escherichia coli recombinant proteins from inclusion bodies.从包涵体中溶解大肠杆菌重组蛋白。
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Properties of recombinant protein-containing inclusion bodies in Escherichia coli.
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Efficient solubilization, activation, and purification of recombinant Cry45Aa of Bacillus thuringiensis expressed as inclusion bodies in Escherichia coli.在大肠杆菌中以包涵体形式表达的苏云金芽孢杆菌重组Cry45Aa的高效溶解、激活及纯化。
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Penicillin-binding protein 2a of Streptococcus pneumoniae: expression in Escherichia coli and purification and refolding of inclusion bodies into a soluble and enzymatically active enzyme.肺炎链球菌青霉素结合蛋白2a:在大肠杆菌中的表达以及包涵体的纯化和重折叠为可溶性且具有酶活性的酶
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7
Purification and renaturation of recombinant human lymphotoxin (tumour necrosis factor beta) expressed in Escherichia coli as inclusion bodies.在大肠杆菌中作为包涵体表达的重组人淋巴毒素(肿瘤坏死因子β)的纯化与复性
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Recovery of soluble, active recombinant protein from inclusion bodies.从包涵体中回收可溶性活性重组蛋白。
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Renaturation, purification and characterization of streptokinase expressed as inclusion body in recombinant E. coli.在重组大肠杆菌中以包涵体形式表达的链激酶的复性、纯化及特性鉴定
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Efficient solubilization of inclusion bodies.包涵体的高效溶解
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