Abstract:
:Expression of recombinant proteins in Escherichia coli often results in the formation of insoluble inclusion bodies, In case of expression of eukaryotic proteins containing cysteine, which may form disulfide bonds in the native active protein, often nonnative inter- and intramolecular disulfide bonds exist in the inclusion bodies. Hence, several methods have been developed to isolate recombinant eukaryotic polypeptides from inclusion bodies, and to generate native disulfide bonds, to get active proteins. This article summarizes the different steps and methods of isolation and renaturation of eukaryotic proteins containing disulfide bonds, which have been expressed in E. coli as inclusion bodies, and shows which methods originally developed for studying the folding mechanism of naturally occurring proteins have been successfully adapted for reactivation of recombinant eukaryotic proteins.
journal_name
Biotechnol Bioengjournal_title
Biotechnology and bioengineeringauthors
Fischer B,Sumner I,Goodenough Pdoi
10.1002/bit.260410103subject
Has Abstractpub_date
1993-01-05 00:00:00pages
3-13issue
1eissn
0006-3592issn
1097-0290journal_volume
41pub_type
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journal_title:Biotechnology and bioengineering
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