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pubmed:abstractText |
Circulating M antigen, specific for genus Schistosoma, was previously described in serum, urine, patients' milk, and in serum and urine of animals infected by S. mansoni. The M antigen was thermostable and soluble in trichloroacetic acid. It was not hydrolyzed by protease, ribonuclease, amylase, or neuraminidase but destroyed by sodium metaperiodate. In the present study, we have purified the M ag by using trichloroacetic acid solubility, DEAE Sephadex, and immunoadsorption. The M ag showed a neutral electric charge, a m.w. heterogeneity, and was only stained by periodic acid-Schiff. The composition study revealed M ag was a glycoprotein with a polysaccharide moiety (63% of the molecules) particularly rich in galactose, fucose, glucosamine, and mannose, and with a high molecular ratio of serine and threonine. The presence of O-glycosidic linkage allowed M ag to be considered as a mucin or a mucus glycoprotein-like component. It was localized in the cell wall of the gut of adult worms.
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