Effect of glutaredoxin and protein disulfide isomerase on the glutathione-dependent folding of ribonuclease A.

@article{Ruoppolo1997EffectOG,
  title={Effect of glutaredoxin and protein disulfide isomerase on the glutathione-dependent folding of ribonuclease A.},
  author={Margherita Ruoppolo and Johanna Lundstr{\"o}m-Ljung and Fabio Talamo and Pietro Pucci and Gennaro Marino},
  journal={Biochemistry},
  year={1997},
  volume={36 40},
  pages={12259-67}
}
Protein folding, associated with oxidation and isomerization of disulfide bonds, was studied using reduced and denatured RNase A (rd-RNase A) and mixed disulfide between glutathione and reduced RNase A derivative (GS-RNase A) as starting materials. Folding was initiated by addition of free glutathione (GSH + GSSG) and was monitored by electrospray mass spectrometry (ESMS) time-course analysis and recovery of the native catalytic activity. The ESMS analysis permitted both the identification and… CONTINUE READING