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Presence of reduced type 1 copper in ceruloplasmin as revealed by reaction with hydrogen peroxide.
Biochem Int. 1984 Jan; 8(1):35-9.BI

Abstract

The reaction of hydrogen peroxide with ox or sheep ceruloplasmin leads to approximately 10% increase of the optical absorption band at 610 nm and of the Type 1 EPR signal. No inactivation or denaturation of the protein is apparent up to 15 H2O2 molar excess. Oxygen is able to restore about 50% of the Type 1 copper absorption in ascorbate-reduced ceruloplasmin, while the other half is recovered after addition of H2O2. It appears that H2O2 undergoes a specific redox reaction with ceruloplasmin, which reveals a fraction of the total copper to be present in the native protein as reduced copper. This fraction is apparently Type 1 copper, while Type 2 is not affected by H2O2.

Authors

Calabrese L
No affiliation info available
Leuzzi U
No affiliation info available

MeSH

AnimalsCattleCeruloplasminCopperElectron Spin Resonance SpectroscopyHydrogen PeroxideKineticsOxidation-ReductionSheepSpectrophotometry

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

6089818

Citation

Calabrese, L, and U Leuzzi. "Presence of Reduced Type 1 Copper in Ceruloplasmin as Revealed By Reaction With Hydrogen Peroxide." Biochemistry International, vol. 8, no. 1, 1984, pp. 35-9.
Calabrese L, Leuzzi U. Presence of reduced type 1 copper in ceruloplasmin as revealed by reaction with hydrogen peroxide. Biochem Int. 1984;8(1):35-9.
Calabrese, L., & Leuzzi, U. (1984). Presence of reduced type 1 copper in ceruloplasmin as revealed by reaction with hydrogen peroxide. Biochemistry International, 8(1), 35-9.
Calabrese L, Leuzzi U. Presence of Reduced Type 1 Copper in Ceruloplasmin as Revealed By Reaction With Hydrogen Peroxide. Biochem Int. 1984;8(1):35-9. PubMed PMID: 6089818.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Presence of reduced type 1 copper in ceruloplasmin as revealed by reaction with hydrogen peroxide. AU - Calabrese,L, AU - Leuzzi,U, PY - 1984/1/1/pubmed PY - 1984/1/1/medline PY - 1984/1/1/entrez SP - 35 EP - 9 JF - Biochemistry international JO - Biochem Int VL - 8 IS - 1 N2 - The reaction of hydrogen peroxide with ox or sheep ceruloplasmin leads to approximately 10% increase of the optical absorption band at 610 nm and of the Type 1 EPR signal. No inactivation or denaturation of the protein is apparent up to 15 H2O2 molar excess. Oxygen is able to restore about 50% of the Type 1 copper absorption in ascorbate-reduced ceruloplasmin, while the other half is recovered after addition of H2O2. It appears that H2O2 undergoes a specific redox reaction with ceruloplasmin, which reveals a fraction of the total copper to be present in the native protein as reduced copper. This fraction is apparently Type 1 copper, while Type 2 is not affected by H2O2. SN - 0158-5231 UR - https://www.unboundmedicine.com/medline/citation/6089818/Presence_of_reduced_type_1_copper_in_ceruloplasmin_as_revealed_by_reaction_with_hydrogen_peroxide_ DB - PRIME DP - Unbound Medicine ER -