jacalin/arachis hypogaea

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Further characterization of the saccharide specificity of peanut (Arachis hypogaea) agglutinin.

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2-Dansylamino-2-deoxy-D-galactose (GalNDns) has been shown to bind to peanut (Arachis hypogaea) agglutinin (PNA) in a saccharide-specific manner. This binding was accompanied by a five-fold increase in the fluorescence of GalNDns. The interaction was characterized by an association constant of 0.15

Characterization of glycoconjugate expression during development of Meckel's cartilage in the rat.

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The staining patterns of 24 biotinylated lectins were analyzed in serial sections of the mandible of 13- to 21-day-old rat embryos by means of the avidin-biotin-peroxidase method. A ubiquitous distribution of binding sites was demonstrated after incubation with Con A (Canavalia ensiformis), DSL

Characterizing the glycocalyx of poultry spermatozoa: II. In vitro storage of Turkey semen and mobility phenotype affects the carbohydrate component of sperm membrane glycoconjugates.

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The turkey sperm glycocalyx is known to contain residues of sialic acid, alpha-mannose/alpha-glucose, alpha- and beta-galactose, alpha-fucose, alpha- and beta-N-acetyl-galactosamine, monomers and dimers of N-acetyl-glucosamine, and N-acetyl-lactosamine. Potential changes in these carbohydrates

Galectin-1-mediated cell adhesion, invasion and cell death in human anaplastic large cell lymphoma: regulatory roles of cell surface glycans.

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Galectin-1 is known to be one of the extracellular matrix proteins. To elucidate the biological roles of galectin-1 in cell adhesion and invasion of human anaplastic large cell lymphoma, we performed cell adhesion and invasion assays using the anaplastic large cell lymphoma cell line H-ALCL, which

Binding properties of a blood group Le(a+) active sialoglycoprotein, purified from human ovarian cyst, with applied lectins.

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Studies on the structures and binding properties of the glycoproteins, purified from human ovarian cyst fluids, will aid the understanding of the carbohydrate alterations occurring during the biosynthesis of blood group antigens and neoplasm formation. These glycoproteins can also serve as important

Cellular heterogeneity in the membrana granulosa of developing rat follicles: assessment by flow cytometry and lectin binding.

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The hormone-mediated maturation of ovarian follicles is apparently accompanied by position-specific differentiation of cells of the membrana granulosa. We have assessed the extent of this cellular heterogeneity by flow cytometry using a variety of fluorescein isothiocyanate-labeled lectins as

Interaction of a novel Tn (GalNAc alpha 1-->Ser/Thr) glycoprotein with Gal, GalNAc and GlcNAc specific lectins.

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A naturally occurring Tn glycoprotein (Native ASG-Tn) with GalNAc alpha 1-->Ser/Thr as the only carbohydrate side chains, has been prepared from armadillo submandibular glands. In a quantitative precipitin assay, this glycoprotein completely precipitated Maclura pomifera (MPA), Vicia villosa B4

Hypersialylated macromolecular serum immunoglobulin A1 in type 2 diabetes mellitus.

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OBJECTIVE The origin of the elevation of serum immunoglobulin A1 (IgA1) in Type 2 diabetes mellitus (DM) is unsettled. The aim of this study was to address the carbohydrate changes of serum IgA1 from patients with Type 2 diabetes mellitus, as a possible cause of the elevation. METHODS IgA1 was

Idiotypes of pre-existing human anti-carcinoma anti-T and anti-Tn antibodies.

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All humans normally possess antibodies, predominantly IgM, that react specifically with the Thomsen-Friedenreich (T) and the Tn antigens which are present in immunoreactive form on > 85% of all human carcinomas, but not in healthy and otherwise diseased tissues. We report here a serological study of

Differential Expression of O-Glycans in CD4(+) T Lymphocytes from Patients with Systemic Lupus Erythematosus.

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T cells from patients with systemic lupus erythematosus (SLE) show a decreased activation threshold and increased apoptosis. These processes seem to be regulated by glycosylated molecules on the T cell surface. Here, we determined through flow cytometry the expression of mucin-type O-glycans on T

Fraction A of armadillo submandibular glycoprotein and its desialylated product as sialyl-Tn and Tn receptors for lectins.

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Fraction A of the armadillo submandibular glycoprotein (ASG-A) is one of the simplest glycoproteins among mammalian salivary mucins. The carbohydrate side chains of this mucous glycoprotein have one-third of the NeuAc alpha 2-->6GalNAc (sialyl-Tn) sequence and two thirds of Tn (GalNAc

O-glycosylation of α-1-acid glycoprotein of human milk is lactation stage related.

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BACKGROUND Human milk provides a multitude of glycoproteins, including highly glycosylated α-1-acid glycoprotein (AGP), which elicits anti-inflammatory and immunomodulatory properties. The milk AGP glycoforms may provide the breastfed infant with a wide range of biological benefits. Here, we

Interaction of hamster submaxillary sialyl-Tn and Tn glycoproteins with Gal, GalNAc and GlcNAc specific lectins.

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Hamster submaxillary glycoprotein (HSM), one of the simplest glycoproteins among mammalian salivary mucins, is composed of approximately equivalent amounts of protein, hexosamine and sialic acid. The Thr and Ser residues in the protein core account for more than half of all of the amino acid

Alterations in the O-linked glycosylation of IgA1 in children with Henoch-Schönlein purpura.

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OBJECTIVE To examine O-linked glycosylation of serum IgA1 in children with acute Henoch-Schönlein purpura (HSP). METHODS The O-linked oligosaccharides of serum IgA1 from 28 children with acute HSP and 26 control children were examined by enzyme immunoassay using plant lectins with well defined

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