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The neutral glycolipid fraction from mouse-propagated, Schistosoma mansoni adult worms has been investigated as to its chromatographic and antigenic properties, and whether it fulfills the serodiagnostic antigen requirements of sensitivity and specificity in the detection of schistosomiasis. Serological analyses were performed by thin-layer chromatography immunostaining and ELISA. In the acute-phase form of mouse schistosomiasis, the kinetics of development of neutral glycolipid-specific antibody levels was correlated with the intensity of the initial infection and the response was dominated by IgG, as represented by the subclass IgG1. With the experimental animal helminthiases screened, glycolipid antigenicity fulfilled the fundamental traits for a serodiagnostic reagent. In the chronic-phase form of human schistosomiasis mansoni, neutral glycolipid-specific antibody levels were not correlated with the intensity of infection, as estimated from the faecal content of parasite eggs, whilst the isotypic response was dominated by IgM and IgG, the latter represented primarily by IgG1 and secondarily by IgG3. With other human helminthiases, glycolipid antigenicity was incomplete, in that, the specificity was only partially fulfilled. The reason for this incomplete specificity has been clarified, in part, by the detection of cryptic schistosomiasis infections in the cohorts of African patient sera examined.

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Using our VTPES technique cyclopentadienone is generated in the gas phase at 500-600 °C from the three different precursors cyclobutene-3,4-dicarboxylic acid anhydride, o-phenylene sulfite and o-benzoquinone and its PE spectrum is recorded. The PE spectrum and also the PE spectra of the various precursors as well as of the cyclopentadienone dimer are interpreted on the basis of our recently developed PERTCI method (i. e. performing large scale perturbation configuration interaction calculations in connection with selection procedures). The agreement between measured and calculated ionization potentials is good.