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

Abstract

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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