Abstract
ZNF191(243-368), a new human zinc finger protein, probably relates to some hereditary diseases and cancers. To obtain adequate amount of ZNF191(243-368) for the study of its property, structure and function, three different expression systems of inclusion-body, glutathione S-transferase (GST), and hexahistidine (6 X His) were used and compared. Among these systems, the expression level of ZNF191(243-368) was increased in inclusion body system under a higher isopropylthio-β-D-galactoside (IPTG) concentration, but the non-target proteins were also increased more, which made its purification more difficult and the yield lower. The expression of His-tag fusion protein was almost not affected by IPTG concentration, temperature and inducing time. At a high IPTG concentration the highest expression yield for GST fusion protein was obtained. And the fusion proteins can be partially purified by a single affinity chromatography step. The fusion protein systems show advantages for expression of these proteins.
Original language | English (US) |
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Pages (from-to) | 1739-1742 |
Number of pages | 4 |
Journal | Chinese Journal of Chemistry |
Volume | 25 |
Issue number | 11 |
DOIs | |
State | Published - Nov 2007 |
Externally published | Yes |
Keywords
- Affinity chromatography
- Fusion protein
- Isopropylthio-β-D-galactoside
- Protein expression
ASJC Scopus subject areas
- General Chemistry