Abstract
The physical and chemical properties of a hemagglutinin from whole-body homogenates of the cephalochordate, Branchiostoma lanceolatum, are described. The hemagglutinin is proteinaceous since it is precipitated by trichloroacetic acid and ammonium sulphate, and all activity is lost at 60°C or by treating with proteases. Carbohydrate moieties are probably also present since activity is lost after incubation with sodium metaperiodate. Activity is stable over pH 6–10. The agglutinin does not require Ca ++ or Mg ++, and a reduced titer after treatment with 2-mercaptoethanol and urea suggests the presence of both disulphide bonds and noncovalent linkages. Haemagglutination inhibition experiments with 17 saccharides and glycoproteins failed to show clear-cut carbohydrate specificity, with only mucin and fetuin having any inhibitory effect, so that the binding may be complex. Finally, cross-adsorption experiments suggest that only one lectin is present. The function of this lectin, especially in an immunobiological context, remains speculative.
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