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4 rezultatus
A novel glycosylphosphatidylinositol-anchored glycoside hydrolase from Ustilago esculenta functions in β-1,3-glucan degradation.
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A glycoside hydrolase responsible for laminarin degradation was partially purified to homogeneity from a Ustilago esculenta culture filtrate by weak-cation-exchange, strong-cation-exchange, and size-exclusion chromatography. Three proteins in enzymatically active fractions were digested with
Lysozyme of the beet armyworm, Spodoptera exigua: activity induction and cDNA structure.
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Lysozyme of the beet armyworm, Spodoptera exigua, was characterized in its up-regulation pattern, and its cDNA was cloned by RT-PCR using degenerate primers designed from some conserved amino acid regions shared with related lepidopteran species. Lysozyme activity of the non-immunized S. exigua had
Schistosoma mansoni excretory-secretory products stimulate a p38 signalling pathway in Biomphalaria glabrata embryonic cells.
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Following infection with Schistosoma mansoni larvae, haemocytes of resistant Biomphalaria glabrata snails execute a rapid defence during which they migrate towards and encapsulate the parasites. Such immediate and precise responses are thought to depend on signal transduction cascades though the
Biochemical and genetic characterization of β-1,3 glucanase from a deep subseafloor Laceyella putida.
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A β-1,3-glucanase (LpGluA) of deep subseafloor Laceyella putida JAM FM3001 was purified to homogeneity from culture broth. The molecular mass of the enzyme was around 36 kDa as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). LpGluA hydrolyzed curdlan optimally at pH
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