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ulex europaeus/албумин

Врската е зачувана во таблата со исечоци
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Preparation and investigation of Ulex europaeus agglutinin I-conjugated liposomes as potential oral vaccine carriers.

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We prepared and optimized Ulex europaeus agglutinin I (UEAI)-modified Bovine serum albumin (BSA)-encapsulating liposomes (UEAI-LIP) as oral vaccine carriers and examined the feasibility of inducing systemic and mucosal immune responses by oral administration of UEAILIP. The prepared systems were

Ulex europaeus 1 lectin targets microspheres to mouse Peyer's patch M-cells in vivo.

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The interaction of latex microspheres with mouse Peyer's patch membranous M-cells was studied in a mouse gut loop model after the microspheres were coated with a variety of agents. Carboxylated microspheres (diameter 0.5 micron) were covalently coated with lectins Ulex europaeus 1, Concanavalin A,

Albumin and Ricinus communis agglutinin decrease endothelial permeability via interactions with matrix.

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We studied the effects of albumin and the lectin Ricinus communis agglutinin (RCA) on hydraulic conductivity (Lp) of bovine pulmonary microvascular endothelial cell monolayers (BPMVEC) because of the evidence that albumin and RCA can interfere with transendothelial albumin permeability

Targeted delivery of antigens to the gut-associated lymphoid tissues: 2. Ex vivo evaluation of lectin-labelled albumin microspheres for targeted delivery of antigens to the M-cells of the Peyer's patches.

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The purpose of this study was to evaluate the possibility of lectin-coupled microspheres to improve the targeted delivery of protein antigens to the lymphoid tissues of mucosal surfaces. Bovine serum albumin containing acid phosphatase model protein and polystyrene microspheres were coupled with

Application of Ulex europaeus agglutinin I-modified liposomes for oral vaccine: Ex Vivo bioadhesion and in Vivo immunity.

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The conjugation of Ulex europaeus agglutinin I (UEAI) onto surface of liposomes has been demonstrated to effectively improve the intestinal absorption of antigen, subsequently induced strong mucosal and systemic immune responses. In this context, we prepared bovine serum albumin (BSA)-encapsulating

Characteristics of albumin binding to opossum kidney cells and identification of potential receptors.

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Albumin re-absorption in the kidney proximal tubule may be pathophysiological in disease. Opossum kidney (OK) cell monolayers were used to investigate the characteristics of [125I]-labelled albumin binding at 4 degrees C. Two binding sites were identified, one with high affinity (KD 154.8 +/-7 mg/l)

Lectin binding to gp60 decreases specific albumin binding and transport in pulmonary artery endothelial monolayers.

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The effect of albumin binding to cultured bovine pulmonary artery endothelial cell (BPAEC) monolayers on the transendothelial flux of 125I-labelled bovine serum albumin (BSA) was examined to determine its possible role on albumin transcytosis. The transport of 125I-BSA tracer across BPAEC grown on

Studies on lectins. XL. O-glycosyl derivatives of Spheron in affinity chromatography of lectins.

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Free monosaccharides can be used for direct glycosylation of Spheron, a spherical macroporous hydroxyalkyl methacrylate-ethylene dimethacrylate copolymer, in a reaction that proceeds at room temperature in dioxane medium under catalysis of dry HCl or BF3. Derivatives of L-fucose, D-galactose,

Lectins at Interfaces-An Atomic Force Microscopy and Multi-Parameter-Surface Plasmon Resonance Study.

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Lectins are a diverse class of carbohydrate binding proteins with pivotal roles in cell communication and signaling in many (patho)physiologic processes in the human body, making them promising targets in drug development, for instance, in cancer or infectious diseases. Other applications of lectins

Remote morphological changes in the white matter after ischaemic stroke.

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Acute phase of stroke is the focus of most experimental and clinical studies on cerebral ischaemia. The scarcity of data on remote changes led us to examine the morphological pictures of brains after ischaemic insults. We paid special attention to the white matter capillaries. We microscopically

Bystander protein protects potential vaccine-targeting ligands against intestinal proteolysis.

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Endowing mucosal vaccines with ligands that target antigen to mucosal lymphoid tissues may improve immunization efficacy provided that the ligands withstand the proteolytic environment of the gastro-intestinal tract until they reach their destination. Our aim was to investigate whether and how three

Lectin (UEA-1) reaction of capillary endothelium with reference to permeability in autopsied cases of cerebral infarction.

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The relationship between endothelial reactivity to Ulex europaeus agglutinin-1 (UEA-1) and the permeability of the vascular wall in human autopsied cases of cerebral infarction was studied. Sections from the cerebral cortex were reacted with horseradish peroxidase UEA-1 to demonstrate the surface

Mitogenic lectins bind to the antigen receptor on human lymphocytes.

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The specificity of interactions between mitogenic and non-mitogenic lectins and disulfide-linked cell surface receptors on human lymphocytes was explored. Lysates (Nonidet-P40) of surface-radioiodinated tonsil lymphocytes and T lymphoblastoid cells (HPB-ALL) were absorbed with lectin-agarose

Recognition of the blood group H type 2 trisaccharide epitope by 28 monoclonal antibodies and three lectins.

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The patterns of cross-reaction of 30 monoclonal antibodies and three lectins were determined by ELISA with 21 ABH, Ii or Lewis related synthetic oligosaccharides coupled to bovine serum albumin. At least seven main groups of cross-reactive patterns were identified among the antibodies, plus several

Lectin cytochemistry of the lacrimal sac epithelium in experimental dacryocystitis.

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OBJECTIVE To study the glycoconjugates in the lacrimal sac epithelium of Japanese white rabbits with experimentally induced chronic dacryocystitis. METHODS Chronic dacryocystitis was induced by a subcutaneous injection of albumin followed by an injection of Staphylococcus aureus into the lacrimal
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