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7 rezultatov
[Purification of lectin from Paris quadrifolia L. and comparison of its carbohydrate-binding specificity with other lectins of the Liliaceae family].
Samo registrirani uporabniki lahko prevajajo članke
Prijava / prijava
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.
Samo registrirani uporabniki lahko prevajajo članke
Prijava / prijava
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.
Samo registrirani uporabniki lahko prevajajo članke
Prijava / prijava
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.
Samo registrirani uporabniki lahko prevajajo članke
Prijava / prijava
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.
Samo registrirani uporabniki lahko prevajajo članke
Prijava / prijava
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.
Samo registrirani uporabniki lahko prevajajo članke
Prijava / prijava
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.
Samo registrirani uporabniki lahko prevajajo članke
Prijava / prijava
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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