Purification and characterization of a sialidase from Bacteroides fragilis SBT3182.
作者： Hiroshi Tanaka , Fumio Ito , Taisuke Iwasaki
DOI: 10.1016/0006-291X(92)91589-I
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摘要: Abstract A sialidase from Bacteroides fragilis SBT3182 was purified 2,240-fold to apparent homogeneity by ammonium sulfate precipitation and sequential chromatographies on DEAE-Toyopearl 650M, Hydroxyapatite, MonoS Superose6 columns. The N-terminal amino acid sequence of this sialidase, Ala-Asp- X -Ile-Phe-Val-Arg-Glu-Thr-Arg-Ile-Pro-, determined. Substrate specificity enzyme using a variety sialogycoconjugates showed 1.5- 2.2-fold preference for sialyl α2–8 linkages when compared with α2–3 α2–6 bound sialic acids, respectively. native had molecular weight 165kDa, as determined gel filtration chromatography consisted three subunits each 55kDa SDS-polyacrylamide electrophoresis. This optimal activity at pH6.1 colominic substrate.
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