Expression and purification of fusion protein CTP-SOD in Pichia pastoris and antioxidant capacity analysis.
- Author:
Peizhi LI
1
;
Junle REN
;
Ting AN
;
Yan LIU
Author Information
1. School of Life Science, Southwest University, Chongqing 400715, China.
- Publication Type:Journal Article
- MeSH:
Antioxidants;
pharmacology;
Cytoplasm;
drug effects;
metabolism;
Genetic Vectors;
genetics;
HeLa Cells;
Humans;
Intracellular Signaling Peptides and Proteins;
genetics;
metabolism;
Oxidative Stress;
drug effects;
Pichia;
genetics;
metabolism;
Recombinant Fusion Proteins;
biosynthesis;
genetics;
pharmacology;
Signal Transduction;
drug effects;
physiology;
Superoxide Dismutase;
biosynthesis;
genetics;
metabolism
- From:
Chinese Journal of Biotechnology
2010;26(3):324-329
- CountryChina
- Language:Chinese
-
Abstract:
Cytoplasmic transduction peptide (CTP) is a newly designed transduction peptide, by which special molecules can be carried out and localized into cytoplasmic compartment. Superoxide dismutase (SOD) is a protein that is difficult to go into cytoplasm. In this study, CTP-SOD fusion gene was amplified from human cDNA by PCR, and the active recombinant protein was successfully expressed in Pichia pastoris. HeLa cells pretreated with CTP-SOD showed a significantly improved survival against the pyrogallol-induced oxidative stress, suggesting CTP-SOD could cross the cell membrane more efficiently and protect cells from oxidative stress.
