vicia graminea/carbohydrate

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Preliminary investigation of the structure of the carbohydrate component of Vicia graminea lectin, a plant glycoprotein.

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Purified Vicia graminea lectin, isolated from seeds, was found to contain D-mannose, 2-acetamido-2-deoxy-D-glucose, L-fucose, D-galactose, and D-xylose in the molar ratios approximately 3.9:1.5:1.2:1.1:1.0. The oligosaccharides, obtained after hydrazinolysis of Vg-lectin, were N-reacetylated,

[Properties of a hemagglutinin isolated from the seeds of Vicia graminea].

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A lectin is isolated from Vicia graminea seeds; it is purified from a crude extract after a precipitation with ammonium sulfate "DEAE"-cellulose chromatography and "sephadex G 150" gel filtration. Its homogeneity is demonstrated by different methods. It is a glycoprotein with 7.3% of carbohydrates.

[Structural characteristics of the blood group N determinant, tested with anti-N lectin from Vicia graminea].

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Crude extracts of Vicia graminea seeds agglutinate human N erythrocytes as anti-N immunsera. The anti-N lectin is purified after precipitations with ammonium sulphate of crude extracts, DE52 Whatman chromatography and sephadex G150 gel filtration. Its homogeneity is demonstrated by physical and

Purification and characterization of a lectin (plant hemagglutinin) with N blood group specificity from Vicia graminea seeds.

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A lectin with N blood group specificity was isolated from Vicia graminea seeds. This lectin was purified from a crude extract by precipitation with ammonium sulfate, DEAE-cellulose chromatography and Sephadex G-150 gel filtration. Purification steps were followed by increase of specific activity.

Evidence that the major cell suface glycoprotein of the TA3-Ha carcinoma contains the Vicia graminea receptor sites.

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The Vicia graminea lectin receptor of the nonstrain-specific TA3-Ha mammary carcinoma ascites cell of the strain A mouse was shown to be predominantly or exclusively on a large mucin-type surface glycoprotein. TA3-Ha cells adsorbed the lectin in amounts equivalent to 5-9 mg of this glycoprotein/10-9

Effect of periodate oxidation on specific activities and carbohydrate components of human blood group N- and M-specific glycoproteins and glycopeptides.

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Mild as well as strong periodate oxidation of isolated erythrocyte N and M glycoproteins and glycopeptides gave extensive to complete destruction of N-specificities as measured with Vicia graminea extracts and of N- as well as M- activities determined with all but 1 of 8 animal anti-N and 13 anti-M

Biosynthesis of Vicia graminea lectin- and Vicia unijuga lectin-binding glycoproteins in human tumor and nontumor cells and an estimation of its epitope structure.

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We investigated biosynthesis of Vicia graminea lectin (VGA)- and Vicia unijuga lectin (VUA)-binding (Vgu) glycoproteins, which are human malignant tumor-associated antigens, in cultured human tumor and non-tumor cells by pulse-labeling experiments with [35S]-methionine, followed by

Isolation and characterization of a Vicia graminea and Vicia unijuga lectins-binding (Vgu) glycoprotein with Thomsen-Friedenreich (T) activity from human liver metastases of pancreas carcinoma.

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1. Perchloric acid-soluble fraction from liver metastases of pancreas carcinoma of a patient with blood group B, was subjected to a systematic affinity chromatography using Vicia unijuga lectin (VUA) and Arachis hypogaea anti-T lectin (PNA) as immobilized ligands and separated into three fractions,

Carbohydrate composition of peripheral, cultured and leukaemic human lymphocyte plasma membranes.

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Plasma membranes isolated from peripheral blood lymphocytes of normal donors, lymphocytes from patients with chronic lymphatic leukaemia (CLL), a T cell and B cell line (MOLT-3 and RPMI-1788) were analysed and compared for total carbohydrate contents. T cells and peripheral blood lymphocytes

Presence of Vicia graminea lectin- and Vicia unijuga lectin-binding (Vgu) glycoprotein in human amniotic fluid and some of its chemical and serological properties.

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Vicia graminea- and Vicia unijuga-binding glycoprotein (Vgu glycoprotein) has been reported as a malignant tumor-associated antigen, which is found in various kinds of malignant tumor-tissues and ascitic and cyst fluids of malignant tumor patients, but not found in 20 kinds of normal human tissues.

Alkali-labile oligosaccharides from glycoproteins of different erythrocyte and milk fat globule membranes.

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Phenol extraction of horse, sheep, cow, pig and human erythrocyte membranes and human milk fat globule membranes gave glycoprotein fractions, all of which were shown by gas chromatography to contain the reduced disaccharide beta-D-galactosyl (1-3)-N-acetyl-D-galactosaminital after treatment with

Reversible loss in suspension culture of a major cell-surface glycoprotein of the TA3-Ha mouse tumor.

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A major cell-surface glycoprotein of the TA3-Ha ascites mammary adenocarcinoma diminished during transfer from ascites growth to cell growth in suspension culture. A sensitive, hemagglutination-inhibition assay that used a lectin from Vicia graminea seeds indicated approximately a 50% loss after

Studies on the receptors of the MNSs group system.

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Results with modified human red cell membrane sialoglycoproteins indicate that alkali-labile sialic acid and amino groups are parts of the erythrocyte receptor sites recognized by common rabbit and human anti-M and -N sera. The "N" antigen, demonstrable in MM glycoprotein preparations by rabbit

In vivo release of glycoprotein I from the Ha subline of TA3 murine tumor into ascites fluid and serum.

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Previous studies have demonstrated that a unique glycoprotein can be cleaved by trypsin from the plasma membrane of the Ha, but not the St, subline of the TA(3) murine mammary adenocarcinoma. Using an automated quantitative method for measurement of trypsincleaved fragments (glycoprotein fraction I)

[Some chemical and serological properties of non-dialysable fractions of human seminal plasmas].

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Some chemical and serological properties of water-soluble and undialysable fraction (WSF) and water-insoluble and undialysable fraction (WISF) of human seminal plasmas were studied. Both of the fractions contained proteins as the main components and also carbohydrates as minor components, and each

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