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A protease-resistant form of the protein PrP (PrP-res) accumulates in tissues of mammals infected with scrapie, Creutzfeldt-Jakob disease, and related transmissible neurodegenerative diseases. This abnormal form of PrP can aggregate into insoluble amyloid-like fibrils and plaques and has been identified as the major component of brain fractions enriched for(More)
Infrared spectra have been obtained for 12 globular proteins in aqueous solution at 20 degrees C. The proteins studied, which vary widely in the relative amounts of different secondary structures present, include myoglobin, hemoglobin, immunoglobulin G, concanavalin A, lysozyme, cytochrome c, alpha-chymotrypsin, trypsin, ribonuclease A, alcohol(More)
A central aspect of pathogenesis in the transmissible spongiform encephalopathies or prion diseases is the conversion of normal protease-sensitive prion protein (PrP-sen) to the abnormal protease-resistant form, PrP-res. Here we identify porphyrins and phthalocyanines as inhibitors of PrP-res accumulation. The most potent of these tetrapyrroles had IC50(More)
Chronic wasting disease (CWD) is an emerging transmissible spongiform encephalopathy (prion disease) of North American cervids, i.e., mule deer, white-tailed deer, and elk (wapiti). To facilitate in vitro studies of CWD, we have developed a transformed deer cell line that is persistently infected with CWD. Primary cultures derived from uninfected mule deer(More)
Infrared spectra for the carbon monoxide complex with myoglobin isolated as the oxygenyl species from bovine heart muscle were carefully examined in the C--O stretch region as either the pH or the temperature was varied. Deconvolutions of these spectra into bands of Gaussian shape suggest the presence of four bands near 1938(I), 1944(II), 1954(III), and(More)
The stable binding of nitric oxide to both Cu+B and Fe2+a3 in cytochrome c oxidase is shown in infrared spectra. The N-O stretch band for Fe2+a3-NO at 1610 cm-1 is similar to the band for MbNO at 1612 cm-1. The Cu+B-NO band is at 1700 cm-1. Thus, electron donation from metal to NO is greater with Fe2+a3 than Cu+B. However, the affinity for NO is only(More)
Subunit V, one of the nuclear-coded subunits of yeast cytochrome c oxidase, has two isoforms, Va and Vb. These alter the in vivo intramolecular rates of electron transfer within the holoenzyme (Waterland, R. A., Basu, A., Chance, B., and Poyton, R. O. (1991) J. Biol. Chem. 266, 4180-4186). The isozyme with Vb has a higher turnover rate and a higher(More)