Fast-reacting Thiols in Rat Hemoglobins Can Intercept Damaging Species in Erythrocytes More Efficiently Than Glutathione
Open Access
- 1 July 1998
- journal article
- Published by Elsevier
- Vol. 273 (30) , 19198-19206
- https://doi.org/10.1074/jbc.273.30.19198
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- The interpretation of protein structures: Estimation of static accessibilityPublished by Elsevier ,2004
- Thiol groups in proteins as endogenous reductants to determine glutathione-protein mixed disulphides in biological systemsBiochimica et Biophysica Acta (BBA) - General Subjects, 1995
- Satisfying Hydrogen Bonding Potential in ProteinsJournal of Molecular Biology, 1994
- Hemoglobins with multiple reactive sulphydryl groups: The reaction of dog hemoglobin with 5,5′-dithiobis (2-nitrobenzoate)Protein Journal, 1993
- The MIDAS display systemJournal of Molecular Graphics, 1988
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983
- Identification and quantitation of glutathione in hepatic protein mixed disulfides and its relationship to glutathione disulfideBiochemical Pharmacology, 1983
- Sensitivity of Hemoglobin Thiol Groups within Red Blood Cells of Rat during Oxidation of GlutathioneEuropean Journal of Biochemistry, 1977
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970