The behavior of holo- and apo-forms of bovine superoxide dismutase at low pH
- 1 November 1975
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure
- Vol. 412 (1) , 26-38
- https://doi.org/10.1016/0005-2795(75)90336-0
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Bovine Erythrocyte Superoxide DismutaseJournal of Biological Chemistry, 1974
- Bovine Erythrocyte Superoxide DismutasePublished by Elsevier ,1974
- Oxidation-reduction properties of bovine erythrocyte superoxide dismutaseBiochemistry, 1973
- Studies on the Reconstitution of Bovine Erythrocyte Superoxide DismutaseJournal of Biological Chemistry, 1973
- Studies on the reconstitution of bovine erythrocyte superoxide dismutase: III. Evidence for a strong interdependence between Cu2+ and Zn2+ binding in the expression of the spectroscopic properties of the native protein and for a close proximity of the Zn2+ and Cu2+ sitesBiochimica et Biophysica Acta (BBA) - Protein Structure, 1973
- Metal sites of copper proteins. III. Symmetry of copper in bovine superoxide dismutase and its functional significanceBiochemistry, 1972
- Metal sites of copper proteins. Ligands of copper in hemocupreinBiochemistry, 1971
- Manifestations of the tertiary structures of proteins in high-frequency nuclear magnetic resonanceJournal of the American Chemical Society, 1967
- NMR-Relaxation Mechanisms of O17 in Aqueous Solutions of Paramagnetic Cations and the Lifetime of Water Molecules in the First Coordination SphereThe Journal of Chemical Physics, 1962
- USE OF GLASS ELECTRODES TO MEASURE ACIDITIES IN DEUTERIUM OXIDE1,2The Journal of Physical Chemistry, 1960