Chronic wasting disease in elk might be a threat to human health.

No abstract

Simultaneous analysis of sialic acids has been a challenging target, because sialic acids having N- or O-acetyl, glycolyl, and sulfonic acid ester groups are labile during their release from carbohydrate chains and analytical procedures. In the present paper, we propose a method using high-performance liquid chromatography coupled with eletrospray ionization mass spectrometry (HPLC-ESI-MS). The method was evaluated by applying to the analysis of sialic acids in various tissues, especially digestive organs in mice and rats. The method was based on the in situ precolumn derivatization of sialic acids after releasing them by hydrolysis. The sialic acids were derivatized with 1,2-diamino-4,5-methylenedioxybenzene to form highly fluorescent quinoxaline derivatives. By using two different hydrolysis conditions (i.e., with 2 M acetic acid and with 0.1 M hydrochloric acid), both total sialic acids and sialic acid distributions were easily determined. We found that sialic acids showed characteristic distributions in the tissues of mice and rats. Further, HPLC-ESI-MS revealed that all the tissues examined in mice and rats commonly contained highly acetylated sialic acids and 8-O-sulfated N-acetylneuraminic acid.

No abstract

The major odor components of finely grated, raw garlic in the air of the human mouth have been studied. Immediately after garlic ingestion, tests of the mouth air of six subjects revealed two major peaks that were positively identified as being ally1 mercaptan and diallyl disulfide; these findings are based on an evaluation of the fragment patterns of a GC-MS analysis and from the actual retention times of these authentic compounds. The ally1 mercaptan level was higher than the level of diallyl disulfide, although both compounds smell like garlic. Our results suggest that after garlic ingestion, ally1 mercaptan is the major garlic-smelling compound in human mouth air, and diallyl disulfide is secondary.

No abstract

The structural details of the essential entity of prion disease, fibril prion protein (PrP(Sc)), are still elusive despite the large body of evidence supporting the prion hypothesis. Five major working models of PrP(Sc) structure, which are not compatible with each other, have been proposed. However, no systematic evaluation has been performed on those models. We devised a method that combined systematic point mutation with threading on knowledge-based amino acid potentials. A comprehensive mutation experiment was performed on mouse prion protein, and the PrP(Sc) conversion efficiency of each mutant was examined. The models were evaluated based on the mutation data by using the threading method. Although the data turned out to be rather more consistent with the models that assumed a conversion of the N-terminal region of core PrP into a β helix than with others, substantial modifications were also required to further improve the current model based on recent experimental results.

No abstract