Expression and purification of human metallothionein-3 beta domain in E-coli

被引：0
|
作者：
Wu, DQ [1 ]
Shen, J [1 ]
Ru, BG [1 ]
机构：
[1] Peking Univ, Natl Lab Prot Engn, Beijing 100871, Peoples R China
来源：
PROTEIN AND PEPTIDE LETTERS | 2000年 / 7卷 / 04期
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D O I：
暂无
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
beta-domain of metallothionein-3/growth inhibitory factor(MT-3/GIF) is crucial to the neuronal growth inhibitory activity of MT-3. The MT-3 beta domain was efficiently expressed as the soluble fusion form with GST protein at a high level which accounted for over 30% total cellular proteins. After the thrombin cleavage and purification, the bioactive recombinant MT-3 beta domain was recovered with the yield of 6 mg/L of medium.
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页码：257 / 263
页数：7
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