The Roles of Glutathione, Thioltransferase, and Glutathione Reductase in the Scission of Sulfur-Sulfur Bonds
- 1 January 1978
- book chapter
- Published by Springer Nature in Proceedings in Life Sciences
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Purification and characterization of cytoplasmic thioltransferase (glutathione:disulfide oxidoreductase) from rat liverBiochemistry, 1978
- The structure of the flavoenzyme glutathione reductaseNature, 1978
- Most of the Coenzyme A in dormant spores of Bacillus megaterium is in disulfide linkage to proteinBiochemical and Biophysical Research Communications, 1977
- Glutathione dependent control of protein disulfide-sulfhydryl content by subcellular fractions of hepatic tissueBiochimica et Biophysica Acta (BBA) - General Subjects, 1977
- Synthesis of a mixed disulfide of egg white lysozyme and glutathione ‐ a model substrate for enzymatic reduction of protein mixed disulfidesFEBS Letters, 1975
- The nature of the enzymatic reduction of the mixed disulfide of coenzyme A and glutathioneFEBS Letters, 1974
- Mechanism of action of enzymes catalyzing thiol—disulfide interchange. Thioltransferases rather than transhydrogenasesFEBS Letters, 1974
- The reduction of the L‐cysteine‐glutathione mixed disulfide in rat liver. involvement of an enzyme catalyzing thiol‐disulfide interchangeFEBS Letters, 1970
- Synthesis and Characterization of the L-Cysteine-Glutathione Mixed Disulfide.Acta Chemica Scandinavica, 1967
- The Disulphide-Reducing Capacity of Liver Mitochondria.Acta Chemica Scandinavica, 1963