Can Recombinant Human Glutathione Peroxidase 1 with High Activity Be Efficiently Produced inEscherichia coli?-Reference-Cited by-同舟云学术

Can Recombinant Human Glutathione Peroxidase 1 with High Activity Be Efficiently Produced inEscherichia coli?

Published:2014-03-20 Issue:9 Volume:20 Page:1524-1530
ISSN:1523-0864
Container-title:Antioxidants & Redox Signaling
language:en
Short-container-title:Antioxidants & Redox Signaling

Author:

Guo Xiao¹,Song Jian²,Yu Yang¹,Wei Jingyan¹³

Affiliation:

1. College of Pharmaceutical Science, Jilin University, Changchun, China.

2. College of Electronic Science and Engineering, Jilin University, Changchun, China.

3. State Key Laboratory of Theoretical and Computational Chemistry, Institute of Theoretical Chemistry, Jilin University, Changchun, China.

Publisher

Mary Ann Liebert Inc

Subject

Cell Biology,Clinical Biochemistry,Molecular Biology,Physiology,Biochemistry,Cell Biology,Clinical Biochemistry,Molecular Biology,Physiology,Biochemistry

Link

http://www.liebertpub.com/doi/pdf/10.1089/ars.2013.5617

Reference9 articles.

1. Structure of the Cathelicidin Motif of Protegrin-3 Precursor

2. Single protein production (SPP) system in Escherichia coli

3. Bacterial Bioreactors for High Yield Production of Recombinant Protein

4. A Comparative Study on the Hydroperoxide and Thiol Specificity of the Glutathione Peroxidase Family and Selenoprotein P

5. Glutathione peroxidase activity in bovine serum and erythrocytes in relation to selenium concentrations of blood, serum and liver

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