Characterization of extracellular neuraminidase produced by Actinomyces pyogenes.
Extracellular neuraminidase from Actinomyces pyogenes could be isolated by ammonium sulfate precipitation, ion exchange chromatography with DEAE cellulose and gel filtration on Ultrogel ACA 54. The purified enzyme had a molecular weight of approximately 50,000 Dalton, a pH optimum at pH 6.0, a temperature optimum at 55 degrees C and a Km value of 1.4 X 10(-4) mol/l with N-acetyl-neuraminlactose as substrate. Preparative isoelectric focussing of the culture supernatant revealed neuraminidase activity mainly at pH 6.5. The enzyme activity was not influenced by metalions or EDTA.
Institut für Bakteriologie, Justus-Liebig-Universität Giessen.
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Schaufuss
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Lämmler
D000190:Actinomyces / Q000201:enzymology*; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D007525:Isoelectric Focusing; D007700:Kinetics; D008970:Molecular Weight; D009439:Neuraminidase / Q000302:isolation & purification* / Q000378:metabolism
D009439:Neuraminidase