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lens culinaris/carbohydrate
Врската е зачувана во таблата со исечоци
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A chimeric lectin formed from Bauhinia purpurea lectin and Lens culinaris lectin recognizes a unique carbohydrate structure.
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Lectins are carbohydrate-binding proteins widely used in biochemical, immunochemical, and histochemical studies. Bauhinia purpurea lectin (BPA) is a leguminous lectin with an affinity for galactose and lactose. Nine amino acids, DTWPNTEWS, corresponding to the amino acid sequence from aspartic
Electron microscopic demonstration of cell surface carbohydrates by means of peroxidase and ferritin complexes of the Lens culinaris lection.
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The use of Lens culinaris lectin for electron microscopic detection of D-mannose,- D-glucose and N-acetyl-D-glucosamine like sites on tumor cells, erythrocytes, erythrocyte ghosts, cultured rat liver cells and various tissues of mice is demonstrated. In addition to Lens culinaris lectin-peroxidase
[Immunologic specific demonstration of cell surface carbohydrates with the lectin of Lens culinaris].
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Determination of the carbohydrate-binding site of Bauhinia purpurea lectin by affinity chromatography.
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To determine the carbohydrate-binding site of Bauhinia purpurea lectin (BPA), a D-galactose- and lactose-binding lectin, a peptide which interacts with lactose was purified from endoproteinase Asp-N digests of BPA by chromatography on a lactose-Sepharose column. It consists of nine amino acids and
A putative role for carbohydrates in sea urchin gastrulation.
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Many studies have examined the effects of lectins on embryonic development. Recently, it has been shown that lectins actually enter the blastocoel of sea urchin embryos without microinjection and bind to specific cell types. The present study was performed to examine the effects of lectins on sea
An immunoglobulin M monoclonal antibody, recognizing a subset of acetylcholinesterase molecules from electric organs of Electrophorus and Torpedo, belongs to the HNK-1 anti-carbohydrate family.
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An immunoglobulin M (IgM) monoclonal antibody (mAb Elec-39), obtained against asymmetric acetylcholinesterase (AChE) from Electrophorus electric organs, also reacts with a fraction of globular AChE (amphiphilic G2 form) from Torpedo electric organs. This antibody does not react with asymmetric AChE
The effects of carcinogenic methylcholanthrene on carbohydrate residues of NK cells.
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The present study examines the effect of methylcholanthrene (MCA), a a carcinogenic polycyclic hydrocarbon, on the carbohydrate receptor determinants (RD) on natural killer (NK) cell surface using the bead-coupled lectin assay. Murine NK cells exhibited different degrees of preferential binding to
Surface carbohydrate changes on Onchocerca lienalis larvae as they develop from microfilariae to the infective third-stage in Simulium ornatum.
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Use was made of seven FITC labelled lectins as tools to investigate the surface of Onchocerca lienalis larvae as they develop through to the infective third-stage in a natural vector, Simulium ornatum. The lectins were derived from Canavalia ensiformis (Con A), Lens culinaris (lentil), Triticum
Quantitative assessment of the multivalent protein-carbohydrate interactions on silicon.
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A key challenge in the development of glycan arrays is that the sensing interface be fabricated reliably so as to ensure the sensitive and accurate analysis of the protein-carbohydrate interaction of interest, reproducibly. These goals are complicated in the case of glycan arrays as surface sugar
Carbohydrates of influenza virus. V. Oligosaccharides attached to individual glycosylation sites of the hemagglutinin of fowl plague virus.
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The carbohydrate side chains of the hemagglutinin of fowl plague virus (A/FPV/Rostock/34 (H7N1] have been localized by a procedure involving fragmentation of the polypeptide with cyanogen bromide and various proteases. The positions of the fragments were determined by radioactive labeling of the
Carbohydrate complexity of the mouse thymocyte Thy-1 glycoprotein as demonstrated by lectin affinity and isoelectric focusing.
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The Thy-1 glycoprotein of mouse thymocytes was analysed with regard to the properties of its carbohydrate part. Of the different lectins tested, partial binding of Thy-1 from membrane extracts was found to Lens culinaris agglutinin (approximately 50%) and wheat germ agglutinin (approximately 25%).
The carbohydrate moieties of suppressor IgG-binding factor released by murine T cells.
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The carbohydrate moieties of murine IgG-binding factor (IgG-BF) were studied using lectins binding N-glycosylated sequences such as Concanavalin A (Con A), Lens culinaris agglutinin (LcA), and wheat germ agglutinin (WGA), and lectins binding O-glycosylated sequences such as peanut agglutinin (PNA)
Carbohydrate structures of human alpha-fetoprotein of patients with hepatocellular carcinoma: presence of fucosylated and non-fucosylated triantennary glycans.
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Chemical structures of the sugar chains of various human alpha-fetoprotein (AFP) species with different affinity for Concanavalin A (Con A) and Lens culinaris agglutinin (LCA) were examined by pyridylamination of their oligosaccharides and stepwise exoglycosidase digestion. Using reversed-phase and
Lectin cytochemistry of carbohydrates on cell membranes of rat cerebellum.
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Wheat germ agglutinin (WGA), Ricinis communis agglutinin (RCA) and Lens culinaris (LC) lectins have been used to characterize carbohydrates of neuronal membrane systems in rat and chick cerebellum. WGA and RCA both label Golgi membrane cisternae on the side of the membrane facing the cisternal space
Carbohydrate composition of beta-core.
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beta-Core is a major component of the hCG-related molecules found in pregnancy urine. We previously have purified the beta-core molecule and have deduced portions of its carbohydrate structure based on lectin binding data. In the present study we used recently developed technology to determine the
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