Paper Information

Journal:   BIOLOGICAL SCIENCES (DANISH-I ZISTI-I IRAN)   SPRING 2009 , Volume 4 , Number 1; Page(s) 55 To 62.
 
Paper: 

CO-EXPRESSION OF CHAPERONES COMBINATION GROEL/ GROES/ DANK/ DNAJ / GRPE AND GROEL/ GROES WITH HUMAN BASIC FIBROBLAST GROWTH FACTOR IN ESCHERCHIA COLI TO REDUCE INSOLUBLE RECOMBINANT PROTEINS

 
 
Author(s):  MOSHTAGHI F.*, MIRZAHOSSEINI H., ALIBOLANDI M.
 
* APARTMENT 8, NO.247, MELLI STREET, NAMJOU AVENUE, TEHRAN, IRAN
 
Abstract: 

Several methods have been suggested or shown to prevent or decrease aggregation during overproduction of recombinant protein in the host cell. One of these methods is coexpression of molecular chaperones. The molecular chaperones help in the mediation of proper folding of the target protein. In this study, we used coexpression of molecular chaperones along with Human Basic Fibroblast Growth Factor in Escherchia coli to reduce insoluble recombinant proteins. Two chaperone combinations comprise; GroEL/ GroES in pGro7 plasmid and GroEL/ GroES/ Dnak/ Dnaj / GrpE in pG-KJE8 plasmid Co-expressed with hbFGF and the effect of molecular chaperone combinations on hbFGF solubility is examined by SDS-PAGE, western blotting and ELISA. Our result proved that Co-expression of GroEL/ GroES/ Dank/ Dnaj / GrpE can act more effective on insoluble rhbFGF reduction.  Correct choice of the chaperone combinations can play an important role in the production of soluble recombinant proteins in Escherichia coli.  DnaK family has important role in the folding of target protein and increase solubility ratio of it while chaperonin increase rhbFGF stability and total yield of target protein.

 
Keyword(s): MOLECULAR CHAPERONE, HBFGF, FOLDING
 
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