dioclea guianensis/éidéime

Sábháiltear an nasc chuig an gearrthaisce

AiltTrialacha cliniciúlaPaitinní

Roghnaigh cineál sórtála

5 torthaí

Neutrophil-infiltrated paw edema induced by mannose-binding Dioclea violacea lectin.

Ní féidir ach le húsáideoirí cláraithe ailt a aistriú

Logáil Isteach / Cláraigh

BACKGROUND The potential edematogenic effect and the pharmacological characterization of a glucose-mannose-binding lectin from Dioclea violacea (DvL) were investigated. METHODS Paw edema was induced with DvL in control animals, and in animals pretreated with glucocorticoid or with blockers of

Rat paw edema and leukocyte immigration induced by plant lectins.

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Logáil Isteach / Cláraigh

Lectins from Dioclea grandiflora (DG) and Canavalia brasiliensis (CB) were compared with Concanavalin A (ConA) for their ability to induce paw edema and peritoneal cell immigration in rats. ConA caused a slight edema with a peak at 1 h after injection, while DG or CB induced a pronounced and

Purification and molecular characterization of a novel mannose-specific lectin from Dioclea reflexa hook seeds with inflammatory activity.

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Logáil Isteach / Cláraigh

A novel lectin present in Dioclea reflexa seeds (DrfL) was discovered and described in this study. DrfL was purified in a single step by affinity chromatography in a Sephadex G-50 column. The lectin strongly agglutinated rabbit erythrocytes and was inhibited by α-methyl-D-mannoside, D-mannose, and

Crystal structure of a pro-inflammatory lectin from the seeds of Dioclea wilsonii Standl.

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Logáil Isteach / Cláraigh

The crystal structure and pro-inflammatory property of a lectin from the seeds of Dioclea wilsonii (DwL) were analyzed to gain a better understanding of structure/function relationships of Diocleinae lectins. Following crystallization and structural determination by standard molecular replacement

Molecular modeling, docking and dynamics simulations of the Dioclea lasiophylla Mart. Ex Benth seed lectin: An edematogenic and hypernociceptive protein.

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Logáil Isteach / Cláraigh

Lectins are proteins, or glycoproteins, capable of reversibly binding to specific mono- or oligosaccharides via a noncatalytic domain. The Diocleinae subtribe presents lectins with high structural similarity, but different effects based on biological activity assays. This variability results from

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Herbal & Natural Medicine

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