[Advances in in vitro refolding of inclusion body proteins].
Overexpression of recombinant proteins in E. coli often results in formation of insoluble, inactive inclusion bodies. These inclusion bodies, which contain the recombinant proteins in a highly enriched form, can be isolated by solid/liquid separation. After solubilization, active proteins can be generated through an appropriate refolding process. Within the last decade, specific strategies and methods have been developed for preparing active recombinant proteins from inclusion bodies. Recent developments in renaturation procedure include the inhibition of aggregation during refolding by the application of low molecular weight additives and matrix-bound renaturation techniques.
Fang
M
M
Institute of Genetics, Chinese Academy of Sciences, Beijing 100101, China.
Huang
H L
HL
D000818:Animals; D001622:Betaine / Q000031:analogs & derivatives* / Q000494:pharmacology; D006801:Humans; D002479:Inclusion Bodies / Q000737:chemistry*; D007202:Indicators and Reagents / Q000494:pharmacology; D018832:Molecular Chaperones / Q000494:pharmacology; D017510:Protein Folding; D020673:Protein Renaturation / Q000187:drug effects; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism
D007202:Indicators and Reagents; D018832:Molecular Chaperones; C111794:NDSB 195; D011994:Recombinant Proteins; D001622:Betaine