Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide.

@article{Holmgren1979ThioredoxinCT,
  title={Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide.},
  author={Arne Holmgren},
  journal={The Journal of biological chemistry},
  year={1979},
  volume={254 19},
  pages={9627-32}
}
  • Arne Holmgren
  • Published 1979 in The Journal of biological chemistry
Thioredoxin from Escherichia coli was shown to catalyze the reduction of insulin disulfides by dithiothreitol. A quantitative assay was developed which measures the rate of insulin reduction spectrophotometrically at 650 nm as turbidity formation from the precipitation of the free insulin B chain. Thioredoxin, at 5 microM concentration, accelerated the reaction between 0.130 mM insulin and 1.0 mM dithiothreitol at pH 7 around 20-fold. The pH optimum of the reaction was 7.5. Thioredoxins from E… CONTINUE READING
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