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Query: UNIPROT:P43026 (lipopolysaccharide)
 62,215 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Normal filter papers were used for specific detection of tiny amounts of antibodies against two penicillin amidase molecular forms from Escherichia coli, monoclonal antibodies of IgG and IgM class against lipopolysaccharide from Citrobacter O36 and IgM antibody against glycoprotein N from human red blood cells. For colour detection of antibodies bound to proper antigens adsorbed on the paper, second antibody-horse radish peroxidase conjugates and hydrogen peroxide with 4-chloronaphthol were applied. The use of filter paper for dot-immunobinding assay of antibodies gave similar results to those obtained with expensive nitrocellulose sheets used by other authors.
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PMID:The use of normal filter paper for "dot-immunobinding assay" of some antibodies. 353 27

The structure of the O-specific polysaccharide of the phenol-soluble cellular lipopolysaccharide of Vibrio anguillarum has been investigated. The studies involved the use of methylation analysis, partial hydrolysis with 48% hydrogen fluoride, Smith degradation, oxidation with chromium trioxide, and comprehensive proton and carbon-13 nuclear magnetic resonance studies, in which one- and two-dimensional experiments were carried out. As a result of these studies it is proposed that the O-specific polysaccharide of Vibrio anguillarum is composed of a regular heteropolymer, i.e., a main chain of (1----4)-linked 3-acetamido-3,6-dideoxy-beta-L-glucose residues alternately substituted through O-2 with side chain residues of 2-acetamido-2,6-dideoxy-alpha-D-glucose, which seem to be substituted through either O-3 or O-4 with propionyl groups (R), as in the following structure. (Formula: see text)
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PMID:Structural elucidation of the O-specific polysaccharide of the phenol-phase soluble lipopolysaccharide of Vibrio anguillarum. 356 67

Strain TA102 of S. typhimurium is a new histidine-requiring mutant, particularly suited to the detection of oxidative mutagens acting at A.T base pairs. 10 oxidizing chemicals, previously tested in strain TA102, were used to evaluate the mutagenic sensitivity of the L-arabinose forward mutation assay of S. typhimurium with respect to those types of mutagens. The mutagenicity of each compound was determined by liquid test, measuring both the frequency of mutants among the survivors and the absolute number of mutants growing in selective plates with traces of D-glucose. Strain BA13 with a wild-type lipopolysaccharide barrier was used as compared to the deep rough derivative strain BA9. The chemicals studied were: bleomycin, t-butyl hydroperoxide, chromium trioxide, cumene hydroperoxide, formaldehyde, glyoxal, glutaraldehyde, hydrogen peroxide, paraquat, and phenylhydrazine. Additionally, ultrasonic oscillation was used as a presumable non-mutagenic lethal control treatment. The L-arabinose forward mutation assay detected the mutagenic activity of all the chemicals under study with a high degree of sensitivity, including paraquat which is unable to revert strain TA102. Positive responses were obtained at doses equivalent to or 10 times lower than the doses detected by strain TA102. The results support the idea that the L-arabinose forward mutation assay could replace the set of specific tester strains used by the histidine reverse mutation assay in general screening for genetic toxins.
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PMID:Oxidative mutagens specific for A-T base pairs induce forward mutations to L-arabinose resistance in Salmonella typhimurium. 389 49

Using C3H/He mice, the antitumor effect and mechanism of lipopolysaccharide (LPS) were studied. The antitumor effect of rabbit serum containing tumor necrosis factor (TNF) was also studied. LPS and TNF, which were administered into mice with tumors, induced hemorrhagic necrosis. LPS and TNF significantly inhibited the tumor growth, as compared with findings in the controls. In the initial stage after LPS administration, dilatation of tumor vessels and thrombus formation in tumor vessels were observed in the histologic study. Tumor blood flow was measured by the hydrogen clearance technique. Tumor blood flow was very small, and was remarkably decreased at 2 hours after LPS administration. These results suggest that hemorrhagic necrosis after LPS administration was due to the decrease of the tumor blood flow. In the study in vitro, YAC-1 cells were damaged but K562 cells were not damaged by rabbit serum containing TNF. In order to find the effect of LPS or TNF on cellular immunity, the delayed type hypersensitivity (DTH) was studied. LPS and TNF prevented the decrease of DTH in the tumor bearing mice on day 25.
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PMID:[Antitumor effects of bacterial lipopolysaccharide and tumor necrosis factor in mice]. 390 2

We investigated the capacity of bacterial endotoxin (lipopolysaccharide, LPS) to modify the oxidative metabolic response to membrane stimulation of human neutrophils. Neutrophils were pretreated for 60 min with LPS, 10 ng/ml, then stimulated by exposure to fixed immune complexes, the chemotactic peptide formyl-methionyl-leucyl-phenylalanine (FMLP), or phorbol myristate acetate. Release of superoxide anion (O-2) was up to 7-times greater in cells preincubated with LPS, depending upon the stimulus used. Consumption of oxygen and release of hydrogen peroxide (H2O2) were similarly increased, using FMLP as stimulus. The enhancement was accompanied by a reduction in lag time and an increase in the rate of the response, but the duration of the oxidative events was not changed. The molecular basis for the augmented oxidative response of LPS-pretreated cells was investigated. Preincubation with LPS at 0 degrees C prevented priming, but preincubation in the presence of cycloheximide or chelation of extracellular calcium ion did not. Neutrophils preincubated with LPS had slightly decreased numbers of binding sites and equivalent binding affinity for radiolabeled FMLP. Possible changes in the enzyme responsible for the oxidative burst were analyzed by studying NADPH-dependent generation of O-2 by particulate fractions from cells preincubated with LPS or buffer, then stimulated before cell disruption. The fraction prepared from LPS-pretreated neutrophils exhibited greater release of O-2 over a wide range of concentrations of NADPH. The calculated apparent Km for NADPH was equivalent in the two fractions, but the Vmax was increased 2.5-fold in the subcellular fraction from LPS-pretreated cells. These results suggest that LPS could increase neutrophil-mediated host defense or the tissue damage associated with endotoxemia by enhancing the generation of oxygen metabolites by neutrophils. These results also support the concept that the neutrophil is not an end-stage cell in regard to function or metabolic activity.
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PMID:Priming of neutrophils for enhanced release of oxygen metabolites by bacterial lipopolysaccharide. Evidence for increased activity of the superoxide-producing enzyme. 609 75

A continuous tissue culture cell line (Karpas line 120), derived from a patient with acute myeloblastic leukemia, not only demonstrates myeloblastic morphology and in vitro expression of several myeloid-specific biochemical markers but also contains Epstein-Barr virus (EBV) nuclear antigen. The present studies demonstrate EBV-genome-specific DNA within the total cellular DNA by molecular hybridization, thus establishing the presence of stable viral genome integration. The cells demonstrate complex coordinated myeloid functions including ingestion, degranulation, and respiratory burst activity. Line 120 cells show a respiratory burst (superoxide and hydrogen peroxide generation and hexosemonophosphate shunt activity) in response to soluble (phorbol myristate acetate) and particulate (latex beads) stimuli, as do normal granulocytes. They ingest complement-opsonized particles (lipopolysaccharide-oil droplets, zymosan, and bacteria), and degranulate in response to them. However, unlike normal granulocytes, the line 120 cells do not demonstrate respiratory burst activity in response to these complementopsonized particles. The dissociation between ingestion of complement-opsonized particles and activation of oxygen-dependent bactericidal activity severely impairs bacterial killing as compared with normal polymorphonuclear phagocytes.
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PMID:Dissociation of opsonized particle phagocytosis and respiratory burst activity in an Epstein-Barr virus-infected myeloid cell line. 624 64

Four procedures were used to evaluate the function of polymorphonuclear leukocytes (PMN) isolated from the blood of cattle experimentally infected with bovine viral diarrhea (BVD) virus: (1) uptake of am emulsion of paraffin oil and Escherichia coli lipopolysaccharide, (2) nitroblue tetrazolium reduction, (3) chemiluminescence, and (4) iodination, or the conversion of iodide to a trichloroacetic acid-precipitable form. A marked impairment of iodination was consistently observed after infection with either a cytopathogenic or a noncytopathogenic strain of BVD virus. A corresponding decrease in paraffin oil uptake, nitroblue tetrazolium reduction, and chemiluminescence was not observed. Serum from BVD virus-infected animals did not depress iodination by normal control PMN in vitro. The iodination, procedure evaluates the activity of the myeloperoxidase, hydrogen peroxide, halide system. This system has potent bactericidal, fungicidal, and virucidal effects. The data indicate that oxidative metabolism by PMN from BVD virus-infected cattle is normal, but that the myeloperoxidase, hydrogen peroxide, halide antibacterial system is impaired. This could be explained by an inhibition of degranulation in PMN from infected cattle. The observed defect in iodination by PMN after BVD virus infection was compounded by a decrease in the number of circulating PMN. The impairment of PMN function may partially explain the increased susceptibility of cattle to secondary bacterial infection during infection with BVD virus.
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PMID:Effects of bovine viral diarrhea virus infection on bovine polymorphonuclear leukocyte function. 626 88

Granule contents from rat polymorphonuclear neutrophils were prepared by extraction with 0.2 M acetate (pH 4), dialyzed against phosphate-buffered saline (pH 7), and tested for bactericidal activity. Bactericidal assays consisted of mixing rat granule extract with 1 x 10(3) to 3 x 10(3) bacterial cells per ml at 37 degrees C for 1 h in a medium suited for bacterial growth. The granule extract demonstrated a distinctive dose-dependent bactericidal activity against outer membrane lipopolysaccharide mutants of Salmonella typhimurium LT-2, independent of added hydrogen peroxide or other active oxygen derivatives. The rough bacterial mutants showed an ordered increase in sensitivity to the rat lysosomal extracts inversely related to the length of their lipopolysaccharide carbohydrate side chains. Fractionation of the rat polymorphonuclear neutrophil granule extract with Sephadex G-100 column chromatography revealed an elution profile containing three major areas (peaks) of protein. Polyacrylamide gel electrophoresis and examination of enzymatic activity showed that these peaks contained myeloperoxidase (peak A), neutral protease (peak B), and lysozyme (peak C) activities. Also observed in peak C were cationic protein species whose cathodal electrophoretic migration was faster than that for lysozyme. Only peak C exhibited a bactericidal activity against the rough mutants of S. typhimurium LT-2 similar to that obtained for the unfractionated granule extract, with susceptibility of the bacterial mutants increasing with a progressive loss of carbohydrate residues in the lipopolysaccharide of the cell wall. The bactericidal activity of the peak C protein fraction was dose dependent. Boiling the unfractionated granule extract or peak C for 30 min had little affect on their antimicrobial activity when reacted against a deep-rough lipopolysaccharide mutant. However, trypsin pretreatment of these fractions significantly reduced their antimicrobial activity for the same mutant chemotype.
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PMID:Bactericidal activity of granule contents from rat polymorphonuclear leukocytes. 629 56

The O-specific polysaccharide of the 0114 antigen (lipopolysaccharide) of Escherichia coli 0114 and oligosaccharides obtained from it by Smith degradation and hydrogen fluoride solvolysis were analyzed, using proton and 13C nuclear magnetic resonance spectroscopy and methylation. The results indicated that the 0114 polysaccharide has the tetrasaccharide repeating unit alpha-N-acetylglucosamine(1 leads to 4) beta-3,6-dideoxy-3-(N-acetyl-L-seryl)aminoglucose(1 leads to 3) beta-ribofuranose(1 leads to 4)galactose. In the polysaccharide the repeating units are joined through beta 1 leads to 3-galactosyl linkages. This structure is compared with that of the serologically cross-reacting Shigella boydii 08 antigen and the serological similarity is discussed.
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PMID:Cell-wall lipopolysaccharide of Escherichia coli 0114:H2. Structure of the polysaccharide chain. 630 15

The cellular sites of H2O2 formation in phagocytizing granulocytes have been identified with cerium chloride. A precipitate was visible in phagosomes and on plasma membranes from intact normal cells in the presence of either 0.71 mM NADH or NADPH. X-ray microanalysis permitted identification of cerium deposition within the phagosomes even in the absence of reduced pyridine nucleotides. Catalase ablated the formation of the reaction product. Intact granulocytes obtained from subjects receiving 1600 units of vitamin E daily for 2 weeks exhibited reaction product in the presence of NADH but not NADPH. Intact cells from subjects treated with vitamin E demonstrated diminished numbers of phagocytic vesicles containing reaction product. During phagocytosis the granulocytes treated with vitamin E consumed oxygen but exhibited significantly reduced rates of hydrogen-peroxide-dependent glucose-1-14C oxidation to 14CO2. Isolated phagocytic vesicles obtained from granulocytes after ingestion of opsonized lipopolysaccharide-paraffin oil droplets contained reaction product when exposed to 0.71 mM NADPH. No reaction product was evident at 0.71 mM NADH but was evident at 2.0 mM NADH. Isolated phagocytic vesicles from the granulocytes of subjects receiving vitamin E exhibited reaction product only in the presence of NADH. These observations suggest that vitamin E interferes with the electron transport chain apparently required for the oxidation of NADPH to form H2O2 in the phagocytizing granulocyte.
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PMID:Vitamin E--a selective inhibitor of the NADPH oxidoreductase enzyme system in human granulocytes. 661 42


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