Structural Characterization of a Water-Soluble Polysaccharide from the Fruiting Bodies of Agaricus bisporus

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Structural Characterization of a Water-Soluble Polysaccharide from the Fruiting Bodies of Agaricus bisporus

An edible fungal polysaccharide termed as ABP was obtained by extraction with hot water, and followed successive chromatographic purification using DEAE-Sepharose Fast Flow column and Sephacryl S-300 High-Resolution column. A symmetrical peak was obtained on high-performance size-exclusion chromatography with an average molecular weight of 5.17 × 104 Da, which was named ABP, and its main compon...

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Antiherpetic mechanism of a sulfated derivative of Agaricus brasiliensis fruiting bodies polysaccharide.

OBJECTIVE To study the anti-herpes simplex virus (HSV) activity of a (1→6)-(1→3)-β-D-glucan isolated from Agaricus brasiliensis fruiting bodies (FR) as well as its chemically sulfated derivative (FR-S). METHODS The antiherpetic activity and mechanism of action was studied by viral plaque assay applying different methodological strategies. RESULTS Although FR presented no in vitro antiherpet...

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Antiherpetic Mechanism of a Sulfated Derivative of Agaricus brasiliensis Fruiting Bodies Polysaccharide

Objective: To study the anti-herpes simplex virus (HSV) activity of a (1 → 6)-(1 → 3)β-D -glucan isolated from Agaricus brasiliensis fruiting bodies (FR) as well as its chemically sulfated derivative (FR-S). Methods: The antiherpetic activity and mechanism of action was studied by viral plaque assay applying different methodological strategies. Results: Although FR presented no in vitro antiher...

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An abundant hydrophobin (ABH1) forms hydrophobic rodlet layers in Agaricus bisporus fruiting bodies.

The SDS-insoluble protein fraction of Agaricus bisporus fruiting bodies was solubilized with trifluoroacetic acid. On SDS-PAGE this fraction was found to contain one abundant protein with an apparent M(r) of 16 kDa. The N-terminal amino acid sequence of this protein was determined and RT-PCR used to isolate a cDNA clone which upon sequencing identified the protein as a typical class I hydrophob...

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ژورنال

عنوان ژورنال: International Journal of Molecular Sciences

سال: 2014

ISSN: 1422-0067

DOI: 10.3390/ijms15010787