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Normal Cytochrome c Oxidase Activity in Prion Protein Gene-Deficient Mice

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Cytochrome c oxidases of prion protein (PrP) gene-deficient (Prnp-/-) and Prnp+/+ mice were examined in vivo and in vitro. Non-invasive near-infrared spectra revealed that oxidation of copper and heme a+a3 in cytochrome c oxidase of Prnp-/- mice was similar to that in Prnp+/+ mice. Biochemical analysis of mitochondrial fractions also supported the results. PrP might not be involved in regulation of cytochrome c oxidase.

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Keywords: Prion protein; copper; cytochrome c oxidase; mitochondria

Document Type: Research Article

Publication date: March 1, 2008

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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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