Human IgG is substrate for the thioredoxin system: differential cleavage pattern of interchain disulfide bridges in IgG subclasses.

@article{Magnusson1997HumanII,
  title={Human IgG is substrate for the thioredoxin system: differential cleavage pattern of interchain disulfide bridges in IgG subclasses.},
  author={Carl G. M. Magnusson and Mikael Bj{\"o}rnstedt and Arne Holmgren},
  journal={Molecular immunology},
  year={1997},
  volume={34 10},
  pages={709-17}
}
Thioredoxin, a 12,000 mol. wt protein with two redox-active cysteine residues, together with thioredoxin reductase and NADPH, may reduce protein disulfides and thereby act as a molecular probe of their structure and reactivity. Interchain and intrachain disulfides are structural elements in all immunoglobulins and therefore potential substrates for the reduced thioredoxin, Trx(SH)2. It was investigated whether such disulfides are cleaved in human polyclonal IgG and IgG subclass myeloma proteins… CONTINUE READING