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concanavalin a/соја
Врската е зачувана во таблата со исечоци
Страница 1 од 51 резултати
Precipitation of galactose-specific lectins by complex-type oligosaccharides and glycopeptides: studies with lectins from Ricinus communis (agglutinin I), Erythrina indica, Erythrina arborescens, Abrus precatorius (agglutinin), and Glycine max (soybean).
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We have recently demonstrated that certain oligomannose and bisected hybrid type glycopeptides and bisected complex type oligosaccharides are bivalent for binding to concanavalin A and can precipitate the lectin [Bhattacharyya, L., Ceccarini, C., Lorenzoni, P., & Brewer, C.F. (1987) J. Biol. Chem.
A comparative evaluation of the level of concanavalin a binding by enriched plasma membrane fractions from developing soybean roots.
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The Concanavalin A (Con A) binding capacity of plasma membranes isolated from meristematic and mature regions of four-day-old soybean (Glycine max L. Merr. cv. Wells) roots was compared. Con A binding was studied using a radiochemical assay with tritiated ((3)H)-Con A and by an electron microscope
Interactions of concanavalin A with glycoproteins. A quantitative precipitation study of concanavalin A with the soybean agglutinin.
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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]. In the present
The isolation and characterization of a root lectin from soybean (Glycine max (L), cultivar Chippewa).
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A lectin has been isolated from the roots of 5-day soybean (Glycine max (L) cultivar Chippewa) seedlings, and its properties have been compared to those of the soybean seed lectin. The sugar-binding activities of the two lectins, both in terms of specific hemagglutinating activity and sugar
Chemical cross-linking immobilized concanavalin A for use in proteomic analyses.
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Lectin affinity chromatography was used to reduce the amount of the abundant glycoprotein beta-conglycinin in total protein samples prepared from developing soybean (Glycine max L. Merrill cv. Jack) seeds. Electrophoretic analysis of both the concanavalin A-Sepharose binding and non-binding fraction
Purification and Developmental Analysis of the Major Anionic Peroxidase from the Seed Coat of Glycine max.
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We show that the majority of peroxidase activity in soybean (Glycine max var Williams 82) seeds is localized to the seed coat. A single isozyme is responsible for this activity and has been purified to electrophoretic homogeneity by successive chromatography on DEAE Sepharose Fast Flow, concanavalin
Topological and functional characterization of the N-glycans of soybean (Glycine max) agglutinin.
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Soybean agglutinin (SBA), is a noncovalently bound tetramer comprised of four identical subunits having a single N-glycan chain, Man9GlcNAc2, that is known to be essential for regeneration of the functional tetrameric structure from unfolded subunits. In this study, SBA was found to have strong
The ATPase of cholinergic synaptic vesicles is associated with sugars.
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The ATPase in synaptic vesicles isolated from Torpedo californica electric organ can be nearly completely solubilized in octaethyleneglycoldodecyl ether containing buffer where it is stable only in a narrow pH range around neutrality. Solubilized ATPase adsorbs to Sepharose columns containing
Characterization of oat vicilin-like polypeptides.
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The 7S and 3S globulin fractions were extracted and characterized from Avena sativa L. seeds which showed similar solubility characteristics and holoprotein size to those of the vicilin fraction in legumes. These holoproteins were characterized by sodium dodecyl sulfate-polyacrylamide gel
Molecular and structural analysis of electrophoretic variants of soybean seed storage proteins.
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Soybean (Glycine max L.) storage proteins are composed mainly of two major components, beta-conglycinin and glycinin. Electrophoretic variants of the beta subunit of beta-conglycinin and the A3 polypeptide of glycinin were detected on SDS-PAGE, and designated them as beta* and A3*, respectively.
Intravenous thyrotropin (TSH)-releasing hormone releases human TSH that is structurally different from basal TSH.
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To determine whether basal TSH differed structurally from TRH-released TSH, the TSH obtained from 11 normal subjects before and after the iv administration of TRH was characterized using lectin-affinity chromatography. TSH was applied to the following lectins: lentil, ricin (both before and after
Expression of glycoconjugates on normally developing and immunologically impaired Hymenolepis diminuta.
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The carbohydrates on the surface of Hymenolepis diminuta were analyzed with gold-labelled lectins, and it was found that the surface coat of the anterior body differs from that of the strobila in its lectin-binding properties. Binding sites for lectins from Abrus precatorius (APA), Arachis hypogaea
Changes in lectin-binding patterns during late fetal development of the rat colon.
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Lectin-binding and histochemical studies were integrated with a morphological description of colon development in rat fetuses to determine whether changes in glycoprotein sugars could be identified with stages of colon organogenesis. At 16 days gestation the colon consisted of a minute lumen
Inhibition of IgE and compound 48/80-induced histamine release by lectins.
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Lectins from Ricinus communis and Glycine max, as well as wheat germ agglutinin and concanavalin A, caused a dose-dependent release of histamine from mast cells present in the mixed peritoneal cells from the rat. In addition, histamine release in an IgE-mediated and a compound 48/80-mediated
Effect of lectins on hepatic clearance and killing of Candida albicans by the isolated perfused mouse liver.
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The isolated perfused mouse liver model was used to study the effects of various lectins on hepatic trapping and killing of Candida albicans. After mouse livers were washed with 20 to 30 ml of perfusion buffer, 10(6) C. albicans CFU were infused into the livers. At the time of recovery, 63% +/- 2%
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