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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.

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

Assignment of lectins specific for D-galactose or N-acetyl-D-galactosamine to two groups, based on their circular dichroism.

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The circular dichroism (CD) spectra of thirteen lectins, most being specific for D-galactose or N-acetyl-D-galactosamine, were compared. Two groupings are proposed on the basis of the CD in the near-ultraviolet region. Group one comprises the lectins from Arachis hypogaea, Glycine max, Phaseolus

[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

Seroconversion of type B to O erythrocytes using recombinant Glycine max alpha-D-galactosidase.

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Recombinant alpha-D-galactosidase (rGal) from soybean (Glycine max) hydrolyzed the immunodominant alpha-D-galactose residue from the B epitope of red blood cells. This converted type B erythrocytes to type O which are "universally" transfusable. Type B red blood cells were obtained from four

Formation of homogeneous carbohydrate-lectin cross-linked precipitates from mixtures of D-galactose/N-acetyl-D-galactosamine-specific lectins and multiantennary galactosyl carbohydrates.

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Quantitative precipitation studies have shown that the Man/Glc-specific lectin concanavalin A (ConA) forms homogeneous (homopolymeric) cross-linked precipitates with individual asparagine-linked oligomannose and bisected hybrid-type glycopeptides in the presence of binary mixtures of 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

Biochemical and functional properties of a lectin purified from korean large black soybeans--a cultivar of glycine max.

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Lectins, a class of proteins that reversibly and non-enzymatically bind specific sugars, have been purified from different kinds of legumes. In this study, a 48-kDa lectin (KBL) was purified from Korean large black soybeans using liquid chromatography. The specific hemagglutinating activity of the

Lectin histochemistry on mucous substances of the taste buds and adjacent epithelia of different vertebrates.

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In the present study carbohydrate residues in taste buds (TBs) and adjacent epithelial formations of a teleostean fish, a frog and the rabbit were detected by means of lectin histochemistry. Biotinylated lectins from Pisum sativum (PSA), Arachis hypogaea (PNA), Dolichos biflorus (DBA), Triticum

Differentiation of Bacillus anthracis and other Bacillus species by lectins.

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Bacillus anthracis was agglutinated by several lectins, including those from Griffonia simplicifolia, Glycine max, Abrus precatorius, and Ricinus communis. Some strains of Bacillus cereus var. mycoides (B. mycoides) were strongly reactive with the lectin from Helix pomatia and weakly reactive with

Inhibition of IgE and compound 48/80-induced histamine release by lectins.

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Lectins from Ricinus communis and Glycine max, as well as wheat germ agglutinin and concanavalin A, caused a dose-dependent release of histamine from mast cells present in the mixed peritoneal cells from the rat. In addition, histamine release in an IgE-mediated and a compound 48/80-mediated

Immunohistochemical investigations on the pyloric glands of the ruin lizard (Podarcis sicula campestris de Betta).

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Mucous cells and enteroendocrine cells of the pyloric region of the ruin lizard (Podarcis sicula campestris De Betta) have been examined by lectin histochemical and immunohistochemical methods. Binding to five plant lectins (Canavalia ensiformis, Con A; Triticum vulgare, wheat germ, WGL; Lotus

Distribution of lectin binding in the testes of the musk shrew, Suncus murinus.

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Distribution of lectin binding in the testis of the musk shrew, Suncus murinus, was investigated by light and transmission electron microscopy. Not only spermatogenic cells but also Sertoli cells bound some lectins. Canavalia ensiformis agglutinin (Con A) and wheat germ agglutinin (WGA, Triticum

Lectin-binding patterns in the spermatogenic cells of the shiba goat testis.

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Lectin-binding patterns in the testis of the sexually mature goat were investigated by light and transmission electron microscopy. Dolichos biflorus agglutinin (DBA) and Griffonia simplicifolia agglutinin-I (GS-I) were negative in the seminiferous epithelium, but soybean (Glycine max) agglutinin

Glycoconjugate expression during Drosophila embryogenesis.

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Glycoproteins and other glycoconjugates present on the surface of many cell types have been identified and assigned various functions. The extent of variation possible in complex glycan structures and the heterogeneity of glycoconjugate expression between two apparently similar cells has been

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