Fluoride and formate interaction with liver and erythrocyte catalases as revealed by solvent-proton magnetic relaxation
- 13 December 1977
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 16 (25), 5465-5470
- https://doi.org/10.1021/bi00644a011
Abstract
No abstract availableThis publication has 8 references indexed in Scilit:
- THE HAEM‐ACCESSIBILITY IN LEGHAEMOGLOBIN OF LUPINUS LUTEUS AS OBSERVED BY PROTON MAGNETIC RELAXATIONInternational Journal of Peptide and Protein Research, 1976
- A nuclear magnetic resonance study of the heme environment in beef liver catalaseBiochemistry, 1976
- Binding of hydrogen donors to horseradish peroxidase: A spectroscopic studyArchives of Biochemistry and Biophysics, 1976
- PROTON MAGNETIC RELAXATION DISPERSION IN HUMAN FLUOROMETHAEMOGLOBIN SOLUTIONSInternational Journal of Peptide and Protein Research, 1976
- Nature of the change produced in catalase by lyophilizationArchives of Biochemistry and Biophysics, 1967
- The Kinetics of Fluoride Binding by Ferric Horse Radish Peroxidase*Biochemistry, 1967
- Immunochemical studies on liver and erythrocyte catalases from cattle, horse, rabbit and humanBiochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1964
- A Study of Crystalline Beef Liver Catalase Dried in the Frozen StateScience, 1943