Abstract
Strains of <i>Erysipelothrix insidiosa </i>were shown to possess neuraminidase. The action of the enzyme on human glycoproteins was demonstrated by immuno-electrophoresis which showed cleavage of acetylneuraminic acid and an increase in the isoelectric point. Immunoelectrophoresis revealed enzyme-induced changes in acid α<sub>1</sub>-glycoprotein, α<sub>1</sub>-antitrypsin, α<sub>2</sub>-macroglobulin, α<sub>2</sub>-HS-glycoprotein, ceruloplasmin, haptoglobin, transferrin and hemopexin. Further proof of the existence of neuraminidase and exclusion of the enzyme neuraminic acidlyase was provided by paper chromatography. Gel filtration of culture broth revealed enzyme activity in two different fractions with distinct molecular weights. The enzyme appears to be an isoenzyme. The isoenzyme of lower molecular weight is produced always with maximal activity after about 100–150 h. In young cultures it is present in small amounts only. The possible pathogenetic role of <i>E. insidiosa </i>neuraminidase is discussed.
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