Anion-binding and the state of copper in caeruloplasmin
- 1 May 1973
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure
- Vol. 310 (1), 38-50
- https://doi.org/10.1016/0005-2795(73)90006-8
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- A method for obtaining linear reciprocal plots with caeruloplasmin and its application in a study of the kinetic parameters of caeruloplasmin substratesBiochemical Journal, 1972
- Comparison of Polypeptide‐Chain Structure of Four Mammalian Ceruloplasmins by Gel Filtration in Guanidine Hydrochloride SolutionsEuropean Journal of Biochemistry, 1972
- Inhibition of Ceruloplasmin by Inorganic AnionsEuropean Journal of Biochemistry, 1972
- Binding of transition metal ions by ceruloplasmin (ferroxidase)Biochemistry, 1971
- Oxidation-Reduction Titrations of Copper Ions in Rhus-LaccaseThe Journal of Biochemistry, 1971
- The state of copper in stellacyanin and laccase from the lacquer tree Rhus verniciferaBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1970
- Purification and properties of laccase and stellacyanin from Rhus verniciferaBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1970
- Evidence of a specific copper(II) in human ceruloplasmin as a binding site for inhibitory anionsBiochimica et Biophysica Acta (BBA) - Protein Structure, 1970
- Ceruloplasmin-Anion InteractionsPublished by Elsevier ,1968
- Inhibitors of caeruloplasminBiochemical Journal, 1967