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Transganglionic transport of the lectin soybean agglutinin (Glycine max) following injection into the sciatic nerve of the adult rat.

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The lectin soybean agglutinin (SBA) from Glycine max binds to small-sized dorsal root ganglion cells and their central terminals in the superficial dorsal horn of the spinal cord. Here we investigated the ability of SBA and SBA conjugated to horseradish peroxidase (SBA-HRP) to trace thin calibre

Overexpression of Nictaba-Like Lectin Genes from Glycine max Confers Tolerance toward Pseudomonas syringae Infection, Aphid Infestation and Salt Stress in Transgenic Arabidopsis Plants.

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Plants have evolved a sophisticated immune system that allows them to recognize invading pathogens by specialized receptors. Carbohydrate-binding proteins or lectins are part of this immune system and especially the lectins that reside in the nucleocytoplasmic compartment are known to be implicated

Precipitation of galactose-specific lectins by complex-type oligosaccharides and glycopeptides: studies with lectins from Ricinus communis (agglutinin I), Erythrina indica, Erythrina arborescens, Abrus precatorius (agglutinin), and Glycine max (soybean).

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We have recently demonstrated that certain oligomannose and bisected hybrid type glycopeptides and bisected complex type oligosaccharides are bivalent for binding to concanavalin A and can precipitate the lectin [Bhattacharyya, L., Ceccarini, C., Lorenzoni, P., & Brewer, C.F. (1987) J. Biol. Chem.

The ribosomal protein P0 of soybean (Glycine max L. Merr.) has antigenic cross-reactivity to soybean seed lectin.

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Soybean (Glycine max L. Merr.) mutants lacking the ability to produce the lectin normally found in soybean seeds (SBL) are designated Le-. A protein of higher molecular weight that cross-reacts with antibodies raised to SBL was found at nearly equivalent levels in roots, hypocotyls, and leaves, and

Role of Lectins in Plant-Microorganism Interactions: II. Distribution of Soybean Lectin in Tissues of Glycine max (L.) Merr.

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Three different assay procedures have been used to quantitate the levels of soybean (Glycine max [L.] Merr.) lectin in various tissues of soybean plants. The assays used were a standard hemagglutination assay, a radioimmunoassay, and an isotope dilution assay. Most of the lectin in seeds was found

Examination of Le and lele Genotypes of Glycine max (L.) Merr. for Membrane-Bound and Buffer-Soluble Soybean Lectin.

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Membrane fractions from seedlings of four soybean [Glycine max (L.) Merr.] lines were examined by radioimmunoassay and hemagglutination assay for the 120,000 dalton soybean lectin. Two of the lines (Sooty and T-102) are genotypically lele and lack buffer-soluble soybean lectin; the remaining two

Spatial and temporal regulation of a soybean (Glycine max) lectin promoter in transgenic cotton (Gossypium hirsutum)

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The activity of a soybean (Glycine max L. Merrill) lectin gene promoter was investigated in transgenic cotton plants (Gossypium hirsutum L.) with the view to using this promoter for the seed-specific alteration of gossypol, a secondary metabolite in cotton that has adverse effects on the nutritional

[Effect of Glycine max lectin on the interaction of prothrombin and erythrocytes].

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Native porcine erythrocytes do not initiate blood coagulation, though even the weak association (Kd = 4,25 +/- 9,35 microM) of prothrombin with their surface which is limited to the projection of two phospholipid polar head groups onto the external cell membrane, exerts a slight but authentic

The isolation and characterization of a root lectin from soybean (Glycine max (L), cultivar Chippewa).

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A lectin has been isolated from the roots of 5-day soybean (Glycine max (L) cultivar Chippewa) seedlings, and its properties have been compared to those of the soybean seed lectin. The sugar-binding activities of the two lectins, both in terms of specific hemagglutinating activity and sugar

Interaction of the soybean (Glycine max) seed lectin with components of the soybean protein body membrane.

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In Leguminosae, lectins occur in the protein bodies which are membrane-lined storage organelles. Studies of the interaction between lectins and other protein body components could provide information about the internal organization of protein bodies and give indication of the biological function of

Evolution and structural diversification of Nictaba-like lectin genes in food crops with a focus on soybean (Glycine max).

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The Nictaba family groups all proteins that show homology to Nictaba, the tobacco lectin. So far, Nictaba and an Arabidopsis thaliana homologue have been shown to be implicated in the plant stress response. The availability of more than 50 sequenced plant genomes provided the opportunity for a

Distribution and evolution of the lectin family in soybean (Glycine max).

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Lectins are a diverse group of proteins that bind specific carbohydrates and are found throughout all kingdoms. In plants, lectins are involved in a range of important processes such as plant defense and stress signaling. Although the genome sequence of Glycine max (soybean) has been published,

Role of intramolecular high-mannose chains in the folding and assembly of soybean (Glycine max) lectin polypeptides: studies by the combined use of spectroscopy and gel-filtration size analysis.

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It was previously reported [Nagai, K. & Yamaguchi, H. (1993) J. Biochem. 113, 123-125] that intramolecular high-mannose chains are essential for reconstitution of soybean lectin from denatured subunits. To obtain more detailed information on the role of the intramolecular high-mannose chains in the

A new mitogenic D-galactosephilic lectin isolated from seeds of the coral-tree Erythrina corallodendron. Comparison with Glycine max (soybean) and Pseudomonas aeruginosa lectins.

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The lectin of Erythrina corallodendron (Caesalpiniaceae) seeds was purified by heating, ammonium sulfate fractionation, and affinity chromatography on acid-treated Sepharose. The purified lectin is similar to the soybean lectin in being a glycoprotein of molecular weight around 110 000 - 120 000 and

A semi-pilot-scale procedure for isolating and purifying soybean (Glycine max) lectin.

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Availability of gram quantities of purified soybean lectin (SBL) to scientists will foster discovery of novel biomedical applications of the lectin and provide the opportunity to investigate the antinutritional effects of SBL in soybean-consuming food animals and poultry. Therefore, a

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