The relative protein disulphide isomerase (PDI) activities of gonadotrophins, thioredoxin and PDI.

@article{Chew1995TheRP,
  title={The relative protein disulphide isomerase (PDI) activities of gonadotrophins, thioredoxin and PDI.},
  author={Carrie Chin Chin. Chew and Thierry Magallon and Nadine Martinat and François Lecompte and Yves Combarnous and J. P. M. Gosling},
  journal={Biochemical Society transactions},
  year={1995},
  volume={23 2},
  pages={
          394S
        }
}
The three-dimensional configuration assumed by a polypeptide chain occurs spontaneously, with or without the participation of molecular chaperones, and is due to the combined interactions of the amino acids in the chain. In the case of disulphide-bond containing proteins, one or more enzymes catalyse the random cleavage and correct reformation of nascent protein disulphide bonds, e.g. protein disulfide-isomerase (PDI). PDI was first discovered in the ninteen sixties and was purified from bovine… CONTINUE READING