How many distinct enzymes are responsible for the several cellular processes involving thiol:protein‐disulphide interchange?
- 15 January 1979
- journal article
- review article
- Published by Wiley in FEBS Letters
- Vol. 97 (2) , 201-210
- https://doi.org/10.1016/0014-5793(79)80085-x
Abstract
No abstract availableKeywords
This publication has 85 references indexed in Scilit:
- Reversible inactivation of tyrosine amino transferase from guinea pig liver by thiol and disulfide compoundsBiochemical and Biophysical Research Communications, 1978
- Early steps in the refolding reaction of reduced ribonuclease AJournal of Molecular Biology, 1978
- Photosynthetic regulatory protein from rabbit liver is identical with thioredoxinFEBS Letters, 1977
- Presence of two different types of protein-disulfide isomerase on cytoplasmic and luminal surfaces of endoplasmic reticulum of rat liver cellsBiochemical and Biophysical Research Communications, 1977
- Intermolecular disulfide bonds at central nervous system synaptic junctionsBiochemical and Biophysical Research Communications, 1976
- Disulfide reduction and sulfhydryl oxidation by microbial enzyme. IV. Some general properties of the purified thiol: Disulfide oxidoreductase from Candida claussenii.Agricultural and Biological Chemistry, 1975
- The single-disulphide intermediates in the refolding of reduced pancreatic trypsin inhibitorJournal of Molecular Biology, 1974
- Pathways of folding of reduced bovine pancreatic ribonucleaseBiochemistry, 1974
- Insulin degradation X. Identification of insulin degrading activity of rat liver plasma membrane as glutathione-insulin transhydrogenaseBiochemical and Biophysical Research Communications, 1973
- The identity of the insulin degrading thiol-protein disulfide oxidoreductase (glutathione-insulin transhydrogenase) with the sulfhydryl-disulfide interchange enzymeFEBS Letters, 1973