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vicia graminea/oligosaccharide
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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,
Interaction of Vicia graminea anti-N lectin with cell surface glycoproteins from erythrocytes with rare blood group antigens.
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The erythrocyte receptors for Vicia graminea (Vg) anti-N lectin have been investigated after 125I-labelling of the purified lectin and binding to membrane components separated by dodecyl sulphate polyacrylamide gel electrophoresis. GP alpha (synonym glycophorin A or MN glycoprotein) and GP delta
Enhanced reaction with Vicia graminea lectin and exposed terminal N-acetyl-D-glucosaminyl residues on a sample of human red cells with Hb M-Hyde Park.
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A sample of polyagglutinable red cells was obtained from a healthy individual (group O, N) possessing a hemoglobin (Hb) variant called Hb M-Hyde Park. The sialic acid content of the individual's red cells is 90 percent of normal, and his cells are agglutinated by monoclonal but not lectin anti-Tn, a
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
Immunochemical characterization of cyanogen bromide degradation products of M and N blood-group glycopeptides.
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The major glycopeptides purified from the tryptic digests of M and N blood-group glycoproteins were degraded with cyanogen bromide into two fragments. The chemical composition and serological activities of the fragments obtained were determined. The results show that M and N blood-group determinants
Modification of amino groups of human-erythrocyte glycoproteins and the new concept on the structural basis of M and M blood-group specificity.
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1. Various kinds of modification of amino groups of M and N blood group glycoproteins abolished their capacity to inhibit rabbit and human anti-M and anit-N sera. 2. The reversible modification of amino groups revealed that M and N blood group activity was restored after the removal of
Effect of modification of amino groups of human erythrocytes on M, N and NVg blood group specificities.
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Modification of amino groups on the surface of human erythrocytes by acetic anhydride and trinitrobenzenesulfonic acid caused loss of agglutinability by human and rabbit anti-M and anti-N sera, was without any effect on agglutinability of N red cells by Vicia graminea agglutinin, and made M cells
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