arisaema flavum/carbohydrate

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Exploration of carbohydrate binding behavior and anti-proliferative activities of Arisaema tortuosum lectin.

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Lectins have come a long way from being identified as proteins that agglutinate cells to promising therapeutic agents in modern medicine. Through their specific binding property, they have proven to be anti-cancer, anti-insect, anti-viral agents without affecting the non-target cells.

Phytochemical screening and antibacterial activity of different solvent extracted samples of Arisaema jacquemontii.

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The current research was carried out to assess the antibacterial activities and phytochemical analysis of the methanol, n-hexane, ethyl acetate, n-butanol soluble fractions and aqueous extracts of the tubers of Arisaema jacquemontii. All the extracts were tested for their antibacterial potential at

A tuber lectin from Arisaema jacquemontii Blume with anti-insect and anti-proliferative properties.

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A tuber lectin from Arisaema jacquemontii Blume belonging to family Araceae was purified by employing a single step affinity chromatography using column of asialofetuin-linked amino activated silica beads and the bound lectin was eluted with 100 mM glycine-HCl buffer pH 2.5. The purified A.

Purification and characterization of a lectin from Arisaema tortuosum Schott having in-vitro anticancer activity against human cancer cell lines.

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A lectin with in-vitro anticancer activity against established human cancer cell lines has been purified by affinity chromatography on asialofetuin-linked amino activated silica beads from the tubers of Arisaema tortuosum, popularly known as Himalayan Cobra lily, a monocot plant from the family

A tuber lectin from Arisaema helleborifolium Schott with anti-insect activity against melon fruit fly, Bactrocera cucurbitae (Coquillett) and anti-cancer effect on human cancer cell lines.

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An anti-insect and anti-cancer lectin has been isolated from Arisaema helleborifolium Schott by affinity chromatography using asialofetuin-linked amino activated silica beads. The bound A. helleborifolium lectin (AHL) was eluted with 100mM glycine-HCl buffer, pH 2.5. It gave a single band on

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