Strategies for production of active eukaryotic proteins in bacterial expression system.
10.1016/S2221-1691(11)60213-X
- Author:
Orawan KHOW
1
;
Sunutcha SUNTRARACHUN
Author Information
1. Queen Saovabha Memorial Institute, Thai Red Cross Society, Bangkok 10330, Thailand.
- Publication Type:Journal Article
- Keywords:
Escherichia coli;
Expression;
Recombinant protein
- MeSH:
Cloning, Molecular;
methods;
Escherichia coli;
genetics;
metabolism;
Gene Expression;
Genetic Vectors;
Glycosylation;
Phosphorylation;
Protein Folding;
Recombinant Proteins;
biosynthesis;
genetics;
metabolism
- From:Asian Pacific Journal of Tropical Biomedicine
2012;2(2):159-162
- CountryChina
- Language:English
-
Abstract:
Bacteria have long been the favorite expression system for recombinant protein production. However, the flaw of the system is that insoluble and inactive proteins are co-produced due to codon bias, protein folding, phosphorylation, glycosylation, mRNA stability and promoter strength. Factors are cited and the methods to convert to soluble and active proteins are described, for example a tight control of Escherichia coli milieu, refolding from inclusion body and through fusion technology.
