Results 251 to 260 of about 74,223 (272)
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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 We have found (unpublished results) that the envelope of Semliki Forest virus (SFV), a group A arbovirus, contains a glycoprotein in which the principal sugars are mannose, galactose and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.
D. C. Ellwood +3 more
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Biochimica et Biophysica Acta (BBA) - Biomembranes, 1983
The concanavalin A receptor from human erythrocyte membranes has been isolated by affinity chromatography using the mild, readily-dialyzable detergent dodecyltrimethylammonium bromide. The purified protein has been reincorporated into large unilamellar phospholipid vesicles using a detergent dialysis technique.
Frances J. Sharom, Christina A. Chicken
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The concanavalin A receptor from human erythrocyte membranes has been isolated by affinity chromatography using the mild, readily-dialyzable detergent dodecyltrimethylammonium bromide. The purified protein has been reincorporated into large unilamellar phospholipid vesicles using a detergent dialysis technique.
Frances J. Sharom, Christina A. Chicken
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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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Photoaffinity Labeling of Concanavalin A
The Journal of Biochemistry, 1975Concanavalin A (Con A) was labeled with p-azidophenyl alpha-D-mannopyranoside under ultraviolet irradiation and the reaction products were separated by affinity chromatography on Sephadex G-100 at pH 5. One of the Con A derivatives thus obtained was characterized as a monovalent dimer at pH 5 and a divalent tetramer at pH 7 by sedimentation equilibrium
Toshiaki Osawa +2 more
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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].
Dipak K. Mandal +2 more
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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].
Dipak K. Mandal +2 more
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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.
George 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 ...
Hiroyuki Ishizaki, Kerry 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 ...
Hiroyuki Ishizaki, Kerry 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.
Jim A. Wright, Howard Ceri
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Immunobiological properties of a concanavalin A derivative
Cellular Immunology, 1978Abstract A monovalent subunit of concanavalin A (Con A) was tested for mitogenic effects on murine splenic lymphocytes in vitro . In contrast to the effects of intact Con A, the monovalent derivative was not mitogenic at any concentration tested. Furthermore, prior exposure of splenic lymphocytes to monovalent Con A rendered the cells refractory to ...
Horowitz, S +3 more
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