Library

Notes: Two patients became infested with Gnathostoma nipponicum after eating raw loach-fish they had caught in a rice field in central Japan. A fragment of Gnathostoma was found in a biopsy from one of them. The sera of both patients reacted with Gnathostoma antigen using indirect immunofluorescence. Scanning electron microscopy was performed on blocks of the paraffin-embedded parasite sample and the viscera of a fish from the same rice field. The risk of eating raw freshwater fish is discussed.

Notes: Summary New compositional and optical data are reported for antimonian and antimonianbismuthian varieties of hemusite from epithermal Au-Ag-Cu deposits in Japan. The empirical formula for the antimonian variety, from the Iriki mine is: (Cu5.83Fe0.14Ag0.01)Σ5.98Mo1.03(Sn0.54Sb0.41Te0.03Bi0.02)Σ1.00(S7.85Se0.15)Σ8.00, and that of the Sb-Bi variety from the Kawazu mine is: (Cu5.84Fe0.14Ag0.01)Σ5.99Mo1.03(Sn0.82Sb0.11Bi0.l0Te0.04)Σ1.07(S7.80Se0.12)Σ7.92. The theoretical formula of hemusite is Cu+ 4Cu2+ 2MO4+Sn4+S8, whilst the most probable formula of the Iriki hemusite is Cu+ 4.5CU2+ 1.5Mo4+Sn4+ 0.5Sb5+ 0.5S8, with Sb5+ substituting for Sn4+ and forming (SbS4)3− tetrahedra as might be expected, given that the metal to sulphur ratio is 1, and given the sphalerite-like structure of the mineral. However Bi3+ cannot be so accommodated, resulting in a deficiency in (S + Se) for Kawazu hemusite. Reflectance spectra for both are compared with those of the tungsten analogue (compositional) of hemusite, kiddcreekite. The relationship between hemusitesensu stricto and these newly reported varieties is discussed in terms of simple and coupled chemical substitutions, and inferences are drawn on the valency of Sb, Bi, Mo and Cu in the hemusite structure.

Notes: Summary Enamel proteins were extracted from the newly formed layer of immature porcine enamel, and the 25 kDa amelogenin, 89 kDa enamelin and 13–17 kDa nonamelogenins were purified. Specific antisera were raised against these proteins. Antibodies specific to the C-terminal region (residues 149–173) of the 25 kDa amelogenin were generated by absorption of the anti-25 kDa amelogenin serum with 20 kDa amelogenin, which contains residues 1–148 of the antigen. Immunoelectrotransfer blotting of the extracted porcine enamel proteins showed that the anti-25 kDa amelogenin serum recognized the 25 kDa and other low and high molecular weight amelogenins. The C-terminal specific anti-25 kDa amelogenin serum reacted only with amelogenins having molecular weights over 23 kDa. The anti-89 kDa enamelin serum recognized the 89 kDa enamelin and lower molecular weight proteins, but neither the amelogenins nor the 13–17 kDa nonamelogenins. The antiserum against the 13–17 kDa nonamelogenins showed no cross reactivity to the 89 kDa enamelin, but recognized higher molecular weight nonamelogenins. In immunohistochemical preparations of the porcine tooth germs, the 25 kDa amelogenin-like immunoreactivity over immature enamel decreased in a gradient from the enamel surface to the middle layer. In the inner layer immunoreactivity was concentrated over the prism sheaths. The C-terminal specific 25 kDa amelogenin-like immunoreactivity was intense at the outer layer of immature enamel and decreased sharply toward the middle layer. Prism sheaths were intensely stained by the antiserum to the 13–17 kDa nonamelogenins. The 89 kDa enamelin-like immunoreactivity over enamel prisms was intense at the outer layer and decreased toward the middle layer. Staining by the anti-89 kDa enamelin serum of prism sheaths was faint. In immature rat incisor enamel, the C-terminal specific 25 kDa amelogenin antiserum demonstrated a staining pattern similar to that in the immature enamel of the pig. Distinct 13–17 kDa nonamelogenin-like and 89 kDa enamelin-like immunoreactivities were found especially in the layer adjacent to the Tomes' process. We conclude that some enamel proteins are degraded soon after their secretion from the secretory ameloblast in the rat and the pig. The specific enamel proteins which reacted with the antiserum to the 13–17 kDa nonamelogenins seem to be involved with the formation of prism sheaths in immature porcine enamel, but not in rat incisor enamel.

Notes: Summary Antigenic variation of pseudorabies virus glycoprotein g II was demonstrated in field isolates by neutralizing monoclonal antibodies. Mutants capable of avoiding neutralization by the monoclonal antibodies specific for glycoproteins g II and g III could be obtained from the parent virus by mutagenesis.

Notes: Abstract Trimethoxybenzenes were oxidized to dimethoxy-p-benzoquinones in fairly good yields (50–60%) with hydrogen peroxide in the presence of heteropolyacid in the solvent of acetic or formic acid.