Characterization of sialidase from Entamoaeba hystolitica and possible pathogenic role in amebiasis


Sialidase from Entamoeba histolytica was purified to apparent electrophoretic homogeneity by chromatography on hydroxyapatite, reactive brown agarose, fetuin/agarose and by fast performance liquid chromatography on a MonoQ column. The enzyme had a molecular mass of 65 kDa, as determined by SDS-PAGE. It had an optimum pH of 5.5 and was maximally active at 37… (More)
DOI: 10.1007/s00436-002-0646-z


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