scilla bifolia/lectin

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[Purification of lectin from Paris quadrifolia L. and comparison of its carbohydrate-binding specificity with other lectins of the Liliaceae family].

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Lectin from rhizomes of Paris quadrifolia I. was purified by affinity chromatography on cross-linked ovomucine with yield of 75 mg per 1 kg of fresh rhizomes. Purified lectin gave a single band on gel disk electrophoresis at pH 4.5 and two bands at pH 8.9. Electrophoresis in gradient 15-20%

Crystallization and preliminary structural studies of Scilla campanulata lectin complexed with alpha1-6 mannobiose.

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Recent work has shown that Scilla campanulata agglutinin from bluebell bulbs has a strong affinity for alpha(1,3)- and alpha(1,6)-linked mannosyl residues and possesses moderate antiretroviral activity. This lectin has been crystallized by the hanging-drop method of vapour diffusion complexed with

Structural characterisation of the native fetuin-binding protein Scilla campanulata agglutinin: a novel two-domain lectin.

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The three-dimensional structure of a 244-residue, multivalent, fetuin-binding lectin, SCAfet, isolated from bluebell (Scilla campanulata) bulbs, has been solved at 3.3 A resolution by molecular replacement using the coordinates of the 119-residue, mannose-binding lectin, SCAman, also from bluebell

Structure of the native (unligated) mannose-specific bulb lectin from Scilla campanulata (bluebell) at 1.7 A resolution.

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The X-ray crystal structure of native Scilla campanulata agglutinin, a mannose-specific lectin from bluebell bulbs and a member of the Liliaceae family, has been determined by molecular replacement and refined to an R value of 0.186 at 1.7 A resolution. The lectin crystallizes in space group P21212

Isolation, characterization, molecular cloning and molecular modelling of two lectins of different specificities from bluebell (Scilla campanulata) bulbs.

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Two lectins have been isolated from bluebell (Scilla campanulata) bulbs. From their isolation by affinity chromatography, they are characterized as a mannose-binding lectin (SCAman) and a fetuin-binding lectin (SCAfet). SCAman preferentially binds oligosaccharides with alpha(1,3)- and

Purification, crystallization and preliminary X-ray analysis of a mannose-binding lectin from bluebell (Scilla campanulata) bulbs.

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Crystals have been grown of a mannose-specific lectin from bluebell (Scilla campanulata) bulbs in a form suitable for X-ray diffraction studies. The crystals, which diffract to high resolution, grew in hanging drops by vapour diffusion, equilibrating with a solution of 70% saturated ammonium sulfate

Scilla campanulata agglutinin crystallized in complex with the trimannoside alpha-D-man-(1-->6)-[alpha-D-man-(1-->3)]-alpha-D-Man.

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The monocot mannose-specific lectin, Scilla campanulata agglutinin (SCA), from bluebell bulbs has a strong affinity for alpha1,3- and alpha1,6-linked mannosyl residues. SCA has been co-crystallized with the trisaccharide alpha-D-mannopyranosyl-(1-->6)-alpha-D-mannopyranosyl-(1-->3)-alpha-D

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