Nuclear magnetic resonance study of the exchangeable histidine protons in bovine and wheat germ superoxide dismutases
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00559a001
Reference21 articles.
1. Superoxide Dismutases in Photosynthetic Organisms
2. Primary structure of human copper-zinc superoxide dismutase. Cysteine - and tryptophan — Containing peptides
3. Isozymes of superoxide dismutase from wheat germ
4. Investigation of the structure of bovine erythrocyte superoxide dismutase by proton nuclear magnetic resonance spectroscopy
5. 1H Nuclear magnetic resonance spectroscopy of yeast copper-zinc superoxide dismutase. Structural homology with the bovine enzyme
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