calystegia sepium/lectin

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Isolation of a novel plant lectin with an unusual specificity from Calystegia sepium.

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A novel plant lectin has been isolated from the rhizomes of Calystegia sepium (hedge bindweed) and partially characterized. The lectin is a dimeric protein composed of two identical non-covalently linked subunits of 16 kDa. Hapten inhibition studies indicate that the novel lectin is best inhibited

Crystallization and preliminary X-ray analysis of a novel plant lectin from Calystegia sepium.

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A mannose-specific lectin from Calystegia sepium has been crystallized by the hanging-drop vapour-diffusion method using ammonium sulfate as precipitant. The needle-shaped crystals are orthorhombic, space group C222(1) with cell dimensions a = 55.2(1), b = 55.9 (1), c = 196.1 (1) A. Fresh crystals

Molecular cloning of the mitogenic mannose/maltose-specific rhizome lectin from Calystegia sepium.

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cDNA clones encoding the mitogenic mannose/maltose-specific lectin from the rhizomes of hedge bindweed (Calystegia sepium) have been isolated and sequenced. Comparison of the deduced amino acid sequence and the molecular weight of the lectin subunit as determined by mass spectrometry indicated that

The crystal structure of the Calystegia sepium agglutinin reveals a novel quaternary arrangement of lectin subunits with a beta-prism fold.

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The high number of quaternary structures observed for lectins highlights the important role of these oligomeric assemblies during carbohydrate recognition events. Although a large diversity in the mode of association of lectin subunits is frequently observed, the oligomeric assemblies of plant

Regulation of gelatinase B (MMP-9) in leukocytes by plant lectins.

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The stimulatory or inhibitory effects of plant lectins on the production of gelatinase A (MMP-2) and gelatinase B (MMP-9) by mononuclear white blood cells was investigated by substrate zymography. Leukocyte cultures from 24-h old buffy coats were spontaneously activated and produced high levels of

The galactose-binding and mannose-binding jacalin-related lectins are located in different sub-cellular compartments.

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A galactose-specific and a mannose-specific lectin of the family of the jacalin-related lectins have been localized by immunofluorescence microscopy. The present localization studies provide for the first time unambiguous evidence for the cytoplasmic location of the mannose-specific jacalin-related

Analysis of the sugar-binding specificity of mannose-binding-type Jacalin-related lectins by frontal affinity chromatography--an approach to functional classification.

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The Jacalin-related lectin (JRL) family comprises galactose-binding-type (gJRLs) and mannose-binding-type (mJRLs) lectins. Although the documented occurrence of gJRLs is confined to the family Moraceae, mJRLs are widespread in the plant kingdom. A detailed comparison of sugar-binding specificity was

Altered glycosylation associated with dedifferentiation of hepatocellular carcinoma: a lectin microarray-based study.

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Altered glycosylation associated with hepatocellular carcinoma (HCC) is well documented. However, few reports have investigated the association between dedifferentiation and glycosylation. Therefore, the aim of this study was to analyze glycosylation associated with dedifferentiation

Carbohydrate binding properties of banana (Musa acuminata) lectin II. Binding of laminaribiose oligosaccharides and beta-glucans containing beta1,6-glucosyl end groups.

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This paper extends our knowledge of the rather bizarre carbohydrate binding poperties of the banana lectin (Musa acuminata). Although a glucose/mannose binding protein which recognizes alpha-linked gluco-and manno-pyranosyl groups of polysaccharide chain ends, the banana lectin was shown to bind to

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