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glycine max lectin/sojabønne
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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
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 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
Direct demonstration of the essential role of the intramolecular high-mannose oligosaccharide chains in the folding and assembly of soybean (glycine max) lectin polypeptides.
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We investigated the role of the intramolecular high-mannose oligosaccharide chains in the folding and assembly of soybean lectin polypeptides. Soybean lectin, dissociated into subunits and completely denatured in 6 M guanidine hydrochloride, was quantitatively reconstituted to the active tetrameric
Comment on a semi-pilot-scale procedure for isolating and purifying soybean (Glycine max) lectin.
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Lectins and the soybean-Rhizobium symbiosis. I. Immunological investigations of soybean lines, the seeds of which have been reported to lack the 120 000 dalton soybean lectin.
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Seeds of six soybean lines (Glycine max (L.) Merr. cv. Columbia, D68-127, Norredo, Sooty, T-102, Wilson 5) have been reported to lack the 120 000 dalton soybean lectin. Immunodiffusion and radioimmunoassay using anti-soybean lectin immunoglobulin failed to detect the lectin in seeds of five lines,
Purification and physicochemical characterization of soyatoxin, a novel toxic protein isolated from soybeans (Glycine max).
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Physicochemical characterization and biological properties of a new toxic protein isolated from soybeans (Glycine max) is reported. The purification procedure consisted basically of ammonium sulfate fractionation, ion exchange, and affinity chromatographies, the latter being used for the removal of
Altered exopolysaccharides of Bradyrhizobium japonicum mutants correlate with impaired soybean lectin binding, but not with effective nodule formation.
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The exact mechanism(s) of infection and symbiotic development between rhizobia and legumes is not yet known, but changes in rhizobial exopolysaccharides (EPSs) affect both infection and nodule development of the legume host. Early events in the symbiotic process between Bradyrhizobium japonicum and
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
Observation of unique cross-linked lattices between multiantennary carbohydrates and soybean lectin. Presence of pseudo-2-fold axes of symmetry in complex type carbohydrates.
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The tetrameric lectin from Glycine max (soybean) (SBA) has been shown to cross-link and precipitate with N-linked multiantennary complex type oligosaccharides containing nonreducing terminal Gal residues (Bhattacharyya, L., Haraldsson, M., & Brewer, C. F. (1988) Biochemistry 27, 1034-1041). In the
Observation of unique cross-linked lattices between multiantennary carbohydrates and soybean lectin. Presence of pseudo-2-fold axes of symmetry in complex type carbohydrates.
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The tetrameric lectin from Glycine max (soybean) (SBA) has been shown to cross-link and precipitate with N-linked multiantennary complex type oligosaccharides containing nonreducing terminal Gal residues (Bhattacharyya, L., Haraldsson, M., & Brewer, C. F. (1988) Biochemistry 27, 1034-1041). In the
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