HIGH EXPRESSION OF RECOMBINANT HUMAN BASIC FIBROBLAST GROWTH FACTOR IN ESCHERICHIA COLI
- VernacularTitle:重组人碱性成纤维细胞生长因子在大肠杆菌中的高效表达
- Author:
Ju WANG
;
Fenyong SUN
;
Xiaojia CHEN
;
Ling ZHANG
;
An HONG
;
- Publication Type:Journal Article
- Keywords:
Human fibroblast growth factor, Escherichia coli ,Expression
- From:
Microbiology
1992;0(02):-
- CountryChina
- Language:Chinese
-
Abstract:
To improve the expression level of non fusion hbFGF in E coli , the coding sequence of human bFGF gene, which had been cloned from primarily cultured human fibroblast, was mutated according to the principle of lowering the GC content and increasing the codon preference After being ligated into pET 3c and transformed into BL21(DE3), the recombinant induced by IPTG Expression level was up to 30% of the total bacterial protein The result indicated that optimizing of the TIR would promote the expression level of recombinant protein
