Abstract:
:For many proteins and peptides, disulfide bridges are prerequisite for their proper biological function. Many commercialized proteins are crosslinked by disulfide bridges that increase their resistance to destructive effects of extreme environment used in industrial processes or protect protein-based therapeutics from rapid proteolytic degradation. Manufacturing of these products must take into account oxidative refolding--a formation of native disulfide bonds by specific pairs of cysteines located throughout a sequence of linear protein. This review describes basic and practical aspects of oxidative folding that should be considered while designing and optimizing manufacturing of proteins using chemical synthesis, semi-synthesis and a recombinant expression.
journal_name
Biotechnol Advjournal_title
Biotechnology advancesauthors
Bulaj Gdoi
10.1016/j.biotechadv.2004.09.002subject
Has Abstractpub_date
2005-01-01 00:00:00pages
87-92issue
1eissn
0734-9750issn
1873-1899pii
S0734-9750(04)00088-6journal_volume
23pub_type
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