Results 251 to 260 of about 22,621,819 (277)
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A Co(III) derivative of concanavalin A
Biochemical and Biophysical Research Communications, 1979Abstract Co(III) has been stoichiometrically incorporated into jack bean concanavalin A. The Co(III) protein still possesses a binding site for an additional divalent transition metal ion which together with Ca(II) can induce the sugar binding ability. No H2O2 oxidation of Co(II) occurs with demetallized concanavalin A activated with Ca(II) and Co(II)
Gerhard R. Munske+4 more
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Adsorption of concanavalin a on human platelets
Annals of Biomedical Engineering, 1982A physiological cell surface adsorption system approach is investigated on human platelets utilizing mathematical modeling. Monodispersed washed platelets are freshly collected in an isotonic buffer as a suspension utilizing a gel filtration technique. Concanavalin A is used as a glycoprotein receptor adsorbate in the adsorption studies.
Anwar B. Bikhazi, Khalil M. Bitar
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Selective binding of RNase B glycoforms by polydopamine-immobilized concanavalin A.
Analytical Chemistry, 2009Glycoanalysis is important in the manufacture and quality control of protein therapeutics. An emerging method for glycoanalysis is the use of lectin arrays.
Todd A Morris+2 more
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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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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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Fractionation of glycopeptides by affinity column chromatography on concanavalin A-sepharose.
Journal of Biochemistry (Tokyo), 1975Using [3H]-labeled oligosaccharides, we found that the presence of at least two alpha-mannosyl residues with free hydroxyl groups at C-3, 4, and 6 is required for oligosaccharides to be related by a concanavalin A-Sepharose column.
S. Ogata, T. Muramatsu, A. Kobata
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The American review of respiratory disease, 1976
Concanavalin A-nonreactive polysaccharide and 2 concanavalin A-reactive polysaccharides of differing concanavalin A affinities that had been purified from culture filtrates of Mycobacterium tuberculosis were subjected to carbohydrate analysis by gas and gas-liquid chromatography.
Thomas M. Daniel, Akira Misaki
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Concanavalin A-nonreactive polysaccharide and 2 concanavalin A-reactive polysaccharides of differing concanavalin A affinities that had been purified from culture filtrates of Mycobacterium tuberculosis were subjected to carbohydrate analysis by gas and gas-liquid chromatography.
Thomas M. Daniel, Akira Misaki
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Cross-linked derivatives of Concanavalin A
1987Publisher Summary This chapter describes methods for the preparation of covalently cross-linked mono-, di-, and tetravalent Concanavalin A derivatives, which do not undergo subunit exchange. Concanavalin A (Con A) is the most widely used lectin in immunology and cell biology. It activates T lymphocytes, leading to cell division, lymphokine production,
Toshiaki Osawa, Masatoshi Beppu
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Inhibition of cytotoxic T lymphocytes with concanavalin A
Cellular Immunology, 1980Abstract Increasing concentrations of concanavalin A (ConA) were found to increasingly inhibit immunologically specific cytotoxic T lymphocyte (CTL)-mediated cytolysis. Even concentrations of ConA that best enabled nonspecific cytolysis were found to inhibit immunologically specific cytolysis by the same population of effector cells.
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