Results 261 to 270 of about 75,255 (281)
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Assemblies of Concanavalin A onto Carboxymethylcellulose
Journal of Nanoscience and Nanotechnology, 2005The immobilization of Concanavalin A, (Con A), onto flat surfaces formed by ultrathin films of carboxymethylcellulose, CMC, silicon wafers or spin-coated poly(methyl methacrylate), (PMMA), was studied by ellipsometry, contact angle measurements and atomic force microscopy (AFM). The formation of Con A monolayer was only observed onto CMC films.
Lizandra B R, Castro, Denise F S, Petri
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Concanavalin A capping in polymorphonuclear leukocytes
European Journal of Pediatrics, 1980Various polymorphonuclear leukocyte (PMN) functions are dependent on an intact intracellular cytoskeleton consisting of the microtubules and the microfilaments. To investigate the microtublule system in PMNs we observed the spontaneous, Colchicine and Diamide induced cap-formation by fluorescence microscopy ion PMNs obtained from children with ...
M, Rister +3 more
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The luminescence properties of concanavalin A
Biochimica et Biophysica Acta (BBA) - Protein Structure, 19751. The luminescence properties of native concanavalin A, both at room temperature and at 77 degrees K, are similar to those of other proteins containing tyrosine and tryptophan. 2. Binding of methyl alpha-D-glucopyranoside to concanavalin A causes a slight reduction of its fluorescence at room temperature. 3.
J N, Miller, G I, Nwokedi
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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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Molecular weight studies on concanavalin A
Biochemical and Biophysical Research Communications, 1971Summary Molecular weight studies have been performed on solutions of Concanavalin A (Con A) at pH values of 5.2, 7.0 and 7.5. The results suggest that Con A exists as a mixture of a species with molecular weight of 30,000 g/mole and higher aggregates.
W D, McCubbin, C M, Kay
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Concanavalin A-Induced Agglutination of Naegleria
The American Journal of Tropical Medicine and Hygiene, 1977Concanavalin A (Con A) agglutinated all Naegleria gruberi strains tested but did not agglutinate any N. fowleri strains tested. Agglutination was time and temperature dependent and Con A concentration and ameba concentration dependent over certain ranges. Agglutination increased to maximum up to 1 h incubation with Con A.
S L, Josephson, R R, Weik, D T, John
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Conformational equilibrium of demetalized concanavalin A
Biochemistry, 1982Concanavalin A (Con A) is known to exist in two conformations [Brown, R. D., III, Brewer, C. F., & Koenig, S. H. (1977) Biochemistry 16, 3883-3896] that differ in their metal ion and saccharide binding properties. The conformation that binds metal ions tightly, and which is associated with saccharide binding, has been designated as "locked" and that ...
R D, Brown, S H, Koenig, C F, Brewer
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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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CONCANAVALIN A‐INDUCED MACROPHAGE AGGREGATING FACTOR
Australian Journal of Experimental Biology and Medical Science, 1981SummaryThe production of the lymphokine activity macrophage aggregating factor (MAgF) by Concanavalin A (Con A)‐pulsed guinea‐pig spleen cells has been investigated. The following observations have been made: (1) MAgF can be assayed quantitatively by measuring the light absorbance of peritoneal exudate cells (PEC) using a spectrophotometer, rather than
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Lektinbindung: Concanavalin A (CON A)
1984Zur Zeit ist bereits ein umfangreiches Spektrum von Lektinen (meist pflanzliche Proteine) bekannt, die spezifisch an Zuckerreste binden [1]. Concanavalin A koppelt an α-D-Mannosly- und α-D-Glucosylgruppen komplexer Carbohydrate, die so markiert werden konnen.
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