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The rapid detection of infectivity of several agents that cause Creutzfeldt-Jakob disease has previously been achieved by assaying for deposits of abnormal prion protein (PrPSc) in follicular dendritic cells in the spleens of transgenic mice carrying the human prion protein gene. In this study, transgenic mice expressing the bovine prion protein were inoculated intraperitoneally with classical (C-type) or atypical L-type bovine spongiform encephalopathies (BSE). Proteinase-resistant PrPSc were detected in the spleens of all transgenic mice at 75 days after inoculation with both types of BSE. Infectivity in PrPSc-positive spleens of the transgenic mice revealed that prions of C- and L-type BSE replicated. These results suggest that bioassay system by the transgenic mice could be useful for the rapid detection of BSE infectivity with discriminating between C- and L-type BSEs.
An “experimental” valence state of metal complexes is
sometime different from the “formal” oxidation state, especially in the species
having redox active ligands. This difference can be seen in biological system,
such as iron(IV)-porphyrin π-cation radical in some heme proteins and
copper(II)-phenoxyl radical in galactose oxidase (GO). Although structural
characterizations of these species by X-ray diffraction methods have been rare
due to their stability, some artificial metal-phenoxyl radical complexes have
been synthesized and successfully characterized by X-ray crystal structure. In
this review, syntheses and X-ray crystal structures of the one-electron
oxidized metal-phenolate complexes, metal- phenoxyl radical,
and high-valent metal phenolate species are discussed.