title: Purification and characterization of a sialidase from Clostridium chauvoei NC08596.
abstract: The sialidase secreted by Clostridium chauvoei NC08596 was purified to apparent homogeneity by ion-exchange chromatography, gel filtration, hydrophobic interaction-chromatography, FPLC ion-exchange chromatography, and FPLC gel filtration. The enzyme was enriched about 10,200-fold, reaching a final specific activity of 24.4 U mg-1. It has a relatively high molecular mass of 300 kDa and consists of two subunits each of 150 kDa. The cations Mn2+, Mg2+, and Ca2+ and bovine serum albumin have a positive effect on the sialidase activity, while Hg2+, Cu2+, and Zn2+, chelating agents and salt decrease enzyme activity. The substrate specificity, kinetic data, and pH optimum of the enzyme are similar to those of other bacterial sialidases.
authors.affiliation: Biochemisches Institut, Christian-Albrechts-Universität, Kiel, Germany.
authors.forename: D
authors.initials: D
authors.lastname: Heuermann
authors.forename: P
authors.initials: P
authors.lastname: Roggentin
authors.forename: R G
authors.initials: RG
authors.lastname: Kleineidam
authors.forename: R
authors.initials: R
authors.lastname: Schauer
mesh_terms: D003013:Clostridium / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D009439:Neuraminidase / Q000737:chemistry / Q000302:isolation & purification*; D013379:Substrate Specificity
chemical_list: D009439:Neuraminidase