Results 121 to 130 of about 34,748 (143)
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Agglutination of an Arbovirus by Concanavalin A
Nature New Biology, 1971MANY enveloped viruses contain carbohydrates as components of glycoproteins1–5 or glycolipid6. We have found (unpublished results) that the envelope of Semliki Forest virus (SFV), a group A arbovirus, contains a glycoprotein in which the principal sugars are mannose, galactose and N-acetylglucos-amine and also a glucose-containing glycolipid.
J D, Oram +3 more
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Modification of the Biological Activities of Concanavalin A by Anti-Concanavalin A
1975Concanavalin A (Con A) bound to cell membrane glycoproteins, may be dissociated from the membrane receptors by competitive ligands such as alpha-methyl-D-mannoside. Addition of antibody to Con A to the system forms complexes of antibody and Con A which are still bound to the membrane receptors.
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Allergenicity of Concanavalin A in Mice
International Archives of Allergy and Applied Immunology, 2009Concanavalin A (Con A) is a potent allergen in certain strains of mice and in particularly the H-2Kk mice, A/J, CBA/H, and C3H/He. Using a dose of 100 μg, the subcutaneous route of injection was the most effective means of inducing high, persistent titers of T cell-dependent circulating anti-Con A reagins without the addition of the classical ‘ΙgE ...
G F, Mitchell, A E, Clarke
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Effect of Concanavalin A on Phagocytosis
Nature New Biology, 1972Concanavalin A has been shown to inhibit phagocytosis by polymorphonuclear leucocytes. The effect is reversed by specific sugars.
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Insulinomimetic homology of concanavalin A
Medical Hypotheses, 1983A striking peptide sequence and three dimensional conformational homology between a portion of insulin and the plant lectin concanavalin A is described. This amino acid sequence has been demonstrated to be essential to the bioactivity of the hormone insulin.
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Structure and Function of Concanavalin A
1975Lectins have been extensively used to analyze a variety of fundamental processes in cell biology. In conjuntion with our studies on the cell surface and mitosis, we have determined the amino acid sequence and three-dimensional struction of concanavalin A (Con A), the mitogenic lectin from the jack bean.
G N, Reeke +5 more
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Biochimica et Biophysica Acta (BBA) - Enzymology, 1980
The reaction of bovine plasma amine oxidase, a glycoprotein, with Concanavalin A in 0.1 M potassium phosphate buffer, pH 7.0 at 25 degrees C were investigated by equilibrium and kinetic methods. A tentative mechanism for the reaction was derived. The Concanavalin A-enzyme interaction was used to show that the carbohydrate is not essential for activity ...
H, Ishizaki, K T, Yasunobu
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The reaction of bovine plasma amine oxidase, a glycoprotein, with Concanavalin A in 0.1 M potassium phosphate buffer, pH 7.0 at 25 degrees C were investigated by equilibrium and kinetic methods. A tentative mechanism for the reaction was derived. The Concanavalin A-enzyme interaction was used to show that the carbohydrate is not essential for activity ...
H, Ishizaki, K T, Yasunobu
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The concanavalin a binding properties of concanavalin A-resistant and -sensitive hamster cell lines
Biochimica et Biophysica Acta (BBA) - Biomembranes, 1977Abstract The binding of labelled concanavalin A to Chinese hamster ovary cells at 4°C exhibits positive cooperativity. Variant cell lines selected for resistance to the cytotoxic effects of the lectin exhibit altered lectin binding properties.
J A, Wright, H, Ceri
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Carbohydrate Research, 1991
Certain oligomannose-type glycopeptides have been previously shown to be bivalent for binding to concanavalin A and capable of precipitating the lectin by forming homogeneous cross-linked lattices [L. Bhattacharyya, M. I. Khan, and C.F. Brewer, Biochemistry, 27 (1988) 8762-8767].
M I, Khan, D K, Mandal, C F, Brewer
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Certain oligomannose-type glycopeptides have been previously shown to be bivalent for binding to concanavalin A and capable of precipitating the lectin by forming homogeneous cross-linked lattices [L. Bhattacharyya, M. I. Khan, and C.F. Brewer, Biochemistry, 27 (1988) 8762-8767].
M I, Khan, D K, Mandal, C F, Brewer
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Concanavalin A and Hemagglutination
Science, 1935J B, Sumner, S F, Howell, A, Zeissig
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