Abstract
The relationship between disulfide bond formation and the exit of proteins from the endoplasmic reticulum may prove critical to maximizing the productivity of eukaryotic expression systems. During the past year, manipulation of redox active foldase enzymes, global inhibition of disulfide formation with dithiothreitol, and removal of specific disulfides via site-directed mutagenesis have all been shown to result in surprising effects on the rate and efficiency of protein secretion in eukaryotic hosts.
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