Results 151 to 160 of about 118,548,475 (188)
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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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Biochimica et Biophysica Acta (BBA) - General Subjects, 1983
Concanavalin A is capable of activating platelets in a concentration-dependent manner as judged by [14C]serotonin secretion from prelabeled platelets. In contrast, succinyl concanavalin A does not induce platelet secretion. Concanavalin A treatment also results in a number of alterations in platelet macromolecules which are presumably associated with ...
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Concanavalin A is capable of activating platelets in a concentration-dependent manner as judged by [14C]serotonin secretion from prelabeled platelets. In contrast, succinyl concanavalin A does not induce platelet secretion. Concanavalin A treatment also results in a number of alterations in platelet macromolecules which are presumably associated with ...
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Concanavalin A is not a ferritin.
BioFactors (Oxford, England), 1991Contrary to recent claims, in vitro evidence has been obtained to establish that Concanavalin A (Con A) is not a ferritin. Four techniques including immunoprecipitation, gel filtration, sucrose density gradient ultracentrifugation and CsCl centrifugation were employed. None of them showed that Con A is a ferritin.
D C, Litzinger, J T, Fleming, J G, Joshi
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