An investigation of a human erythrocyte SOD modified at position 137
- 31 December 1988
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 111 (2) , 714-719
- https://doi.org/10.1021/ja00184a049
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- On the mechanism of action of superoxide dismutase: a theoretical studyJournal of the American Chemical Society, 1984
- A study of the pH dependence of the activity of porcine Cu,Zn superoxide dismutaseBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984
- Spectroscopic studies of copper(II) bound at the native copper site or substituted at the native zinc site of bovine erythrocuprein (superoxide dismutase)Journal of the American Chemical Society, 1982
- Reduced anion-binding affinity of Cu,Zn superoxide dismutases chemically modified at arginineBiochemical and Biophysical Research Communications, 1982
- Determination and analysis of the 2 Å structure of copper, zinc superoxide dismutaseJournal of Molecular Biology, 1982
- A water 17O NMR study of the pH dependent properties of superoxide dismutaseBiochemical and Biophysical Research Communications, 1981
- Some sulfhydryl properties and primary structure of human erythrocyte superoxide dismutaseBiochemistry, 1980
- Chemical modification of arginine at the active site of the bovine erythrocyte superoxide dismutaseBiochemistry, 1979
- Properties of the cupric sites in bovine superoxide dismutase studied by nuclear-magnetic-relaxation measurementsBiochemical Journal, 1979
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951