Nuclear magnetic resonance study of solvent exchange and nuclear Overhauser effect of the histidine protons of bovine superoxide dismutase
- 16 October 1979
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 18 (21) , 4669-4675
- https://doi.org/10.1021/bi00588a030
Abstract
No abstract availableThis publication has 4 references indexed in Scilit:
- Zymogen activation in serine proteinases. Proton magnetic resonance pH titration studies of the two histidines of bovine chymotrypsinogen A and chymotrypsin A.alpha.Biochemistry, 1978
- Investigation of the structure of bovine erythrocyte superoxide dismutase by proton nuclear magnetic resonance spectroscopyBiochemistry, 1977
- Metal sites of copper-zinc superoxide dismutaseBiochemistry, 1977
- Nuclear magnetic resonance and chemical modification studies of bovine erythrocyte superoxide dismutase: evidence for zinc-promoted organization of the active site structureBiochemistry, 1977