Title: Screening and Selection Strategies for Disulfide Isomerase Activity
Abstract: AbstractDisulfide isomerases (EC 5.3.4.1) were first discovered almost 40 years ago by Christian Anfinsen, and have since been shown to occur in numerous organisms from bacteria to man (1). These enzymes play a key role in disulfide bond formation, an essential step in the oxidative folding of secreted proteins. The effort to determine the in vivo function and substrate specificity of disulfide isomerases has been hampered by the fact that, in vitro, the same isomerase enzyme can catalyze protein thiol oxidation, disulfide bond reduction, or disulfide bond rearrangement depending upon the redox conditions (2). Despite decades of studies, the detailed catalytic mechanism of disulfide bond isomerization is still not completely understood. KeywordsPhage ParticleGenetic SelectionHelper PhageRecombinant PhagePhage StockThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
Publication Year: 2003
Publication Date: 2003-11-15
Language: en
Type: article
Indexed In: ['crossref', 'pubmed']
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Cited By Count: 4
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