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Ceruloplasmin, the Unique Multi-Copper Oxidase of Vertebrates

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This review shortly summarizes the structural and functional properties of ceruloplasmin, the blue copper oxidase of vertebrates. Particular emphasis will be put on the unique copper stoichiometry of ceruloplasmin in comparison to all other multi-copper oxidases, and different hypotheses will be discussed to explain the apparently useless redundancy of type 1 copper ions in the vertebrate oxidase.
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Keywords: CERULOPLASMIN; Copper transport; Coprinus cinereus laccase; MULTI-COPPER OXIDASE; aceruloplasminemia; ascorbate oxidase; ascorbate oxidase (C); ferroxidase; multi-copper ferroxidase

Document Type: Review Article

Publication date: 2001-06-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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