Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P43026 (lipopolysaccharide)
 62,215 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Repeated extractions (three times) of an S-form and different R-mutants of S. typhimurium and S. minnesota with urea medium resulted in extracts varying in their chemical composition with respect to protein, lipopolysaccharides, phospholipids and nucleic acids. Protein appeared to be the major component of all the extracts and was present in substantial amounts in the third extract also. With subsequent extractions the lipopolysaccharide and phospholipid contents generally decreased in the R-mutants, but increased in the S-form. The nucleic acid contents always increased with repeated extractions. polypeptide patterns of the materials obtained after repeated extraction showed some differences in case of R-mutants predominantly. Active immunization of mice with these extracts protected them almost to the same extent against S. typhimurium infection. Only in case of one R-mutant a graded decrease in protection could be observed from extract 1 to extract 3. However, the differences in composition of the vaccines based on chemical analysis data and polypeptide pattern could not account for this decrease in protection.
 ...
PMID:Protective activity of extracts from Salmonella-R-mutants against Salmonella typhimurium infection in mice. Influence of repeated extractions on the chemical composition and efficacy of the extracts. 617 87

Homologous antisera were raised against lipopolysaccharides (LPSs) isolated from pyocin 103-sensitive JW31 strain Neisseria gonorrhoeae and its isogenic, pyocin-resistant variant, JW31R. Changes in immunochemical reactivity of LPS antigen associated with pyocin-resistance were examined by enzyme-linked immunosorbent assay, employing homologous and heterologous anti-LPS immune sera. The acquisition of pyocin 103 resistance is accompanied by a loss in LPS antigen reactivity with homologous anti-LPS. The variant LPS of pyocin 103-resistant mutants is immunogenic and displays a new, distinct antigenic specificity shared with other pyocin 103-resistant variant gonococcal strains. The acquisition of pyocin 103 resistance by JW31 strain gonococci is also accompanied by a striking loss of LPS cross-reactivity with antistreptococcal polysaccharide reagents having an antibody combining site specificity directed against the chemically defined lactose polymer from Streptococcus faecalis cell wall and pneumococcal type 14 capsular polysaccharide. When examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and sodium dodecyl sulfate-urea-polyacrylamide gel electrophoresis, JW31 and JW31R LPSs show banding patterns characteristic of microheterogeneous, rough-type LPS devoid of O-side chains. Immunoblot transfer analysis of gel-separated gonococcal LPS antigens shows a difference in the pattern of antibody binding by homologous versus cross-reactive anti-LPS, which suggests a heterogeneity in the distribution of cross-reactive determinants among LPS molecules.
 ...
PMID:Antigenic specificity and heterogeneity of lipopolysaccharides from pyocin-sensitive and -resistant strains of Neisseria gonorrhoeae. 619 64

Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of purified lipopolysaccharide (LPS) from Neisseria gonorrhoeae resulted in the formation of multiple bands. Many of the bands consisted of LPS aggregates, which could be dissociated by treatment with 0.1 M NaOH or by addition of 4 M urea to the separating gel. The unaggregated LPS was usually found in one to three bands toward the bottom of the gels, a result suggesting that a long repeating O antigen is not present on gonococcal LPS. SDS-PAGE of LPS from different LPS serotypes of N gonorrhoeae indicated that structural heterogeneity exists. Antigenic analysis by enzyme-linked immunosorbent assay inhibition of gonococcal LPS extracted with phenol-chloroform-petroleum ether (PCP) and phenol-water revealed that PCP-extracted LPS contained substantially less serotype-specific antigen than did phenol-water-extracted LPS. These results suggest that the PCP and phenol-water methods extract different molecular species of LPS from N gonorrhoeae.
 ...
PMID:Electrophoretic and serological characterization of the lipopolysaccharide produced by Neisseria gonorrhoeae. 620 6

Western Blotting of whole cell preparations of three strains of Proteus mirabilis after separation by electrophoresis on SDS-polyacrylamide gels revealed a complex pattern of antigens. Similar antigen profiles were obtained with isolated outer membranes indicating that the majority of cell surface antigens are located in the outer membrane. Major outer membrane proteins were strongly antigenic and cross-reactive. The highly immunogenic flagella were detected in whole cell preparations and visible in isolated outer membranes. Whereas the protein and flagellar antigens were cross-reactive, lipopolysaccharide (LPS) could only be detected as immunoreactive material using homologous antisera for each strain. The LPS appeared as two broad bands (high and low Mr, respectively) in immunoblots of whole cells, isolated outer membranes and purified LPS. However, isolated LPS could be resolved into multiple sharp bands when 4 M urea was included in the gel system. These discrete bands are assumed to represent differing O antigen chain lengths of the LPS as reported for other Gram-negative organisms.
 ...
PMID:Surface antigens of Proteus mirabilis revealed by electroblotting from sodium dodecyl sulphate-polyacrylamide gels. 637 19

Peptidoglycan sacculi with peptidoglycan-associated proteins were prepared from cell envelopes of Brucella abortus by extraction with sodium dodecyl sulfate (SDS) at 50 degrees C. On extraction of these preparations with SDS at 100 degrees C, a protein was obtained whose removal from peptidoglycan was confirmed by electron microscopy. Incubation of the 50 degrees C SDS-extracted cell envelopes with 50 mM MgCl2 in SDS-2-beta-mercaptoethanol at 37 degrees C also extracted the protein, along with lipopolysaccharide. At temperatures below 60 degrees C, the protein did not bind SDS strongly and had an apparent molecular weight greater than 92,000 in SDS-polyacrylamide gel electrophoresis. At higher temperatures, SDS bound strongly, and the apparent molecular weight was 38,000. Urea at 5 M did not alter the electrophoretic mobility of this 38,000-molecular-weight form. Immunoelectrophoresis in detergents with antisera to cell envelopes, carbohydrate staining of SDS-polyacrylamide gels, and production of anti-lipopolysaccharide antibodies by mice immunized with the purified protein indicated that lipopolysaccharide was present in free and protein-bound forms. Sequential gel filtration in SDS-EDTA and SDS-NaCl removed most lipopolysaccharide. After further purification by preparative SDS-polyacrylamide gel electrophoresis, a gas-liquid chromatographic analysis showed residual lipid tightly associated with the protein. The results suggested that the interactions between matrix proteins and other outer membrane components are stronger in B. abortus than in Escherichia coli, which was used as a control throughout.
 ...
PMID:Isolation, purification, and partial characterization of Brucella abortus matrix protein. 640 96

Addition of pyruvate to growth medium failed to induce the changes in Neisseria gonorrhoeae that have been reported previously. Addition of 3.8 mM sulfite or 1.3 mM sulfite plus 14 mM pyruvate restored the medium's reactivity in a test for cysteine and its ability to induce changes in N. gonorrhoeae. The induced changes that were restored were (i) increased colonial opacity and roughness, (ii) increased sensitivity to killing by normal human serum, and (iii) electrophoretic changes that may represent changes in lipopolysaccharide. Further characterization of the electrophoretic changes showed that the bands were resistant to treatment with proteinase K, that they were not affected by EDTA and urea, and that they were not dependent upon the stage of growth.
 ...
PMID:A role for sulfite in inducing surface changes in Neisseria gonorrhoeae. 643 4

The metabolic fate of an oral dose of 3.5 mmol 15N-labelled nitrate was investigated in young adults. An average of 60% of the 15N-nitrate dose appeared in the urine within 48 h; less than 0.1% appeared in the faeces. Some of the 15N label of nitrate was found in the urine (3%) and faeces (0.2%) in the form of ammonia and urea; the remainder of the dose was attributed to nitrate loss via metabolism to other reduced nitrogen compounds. Studies with germ-free rats indicated that half of the nitrate metabolism is due to mammalian processes. These and previous studies show that not all of the nitrate excreted in the urine is of dietary origin but evolves from endogenous synthesis. An oral dose of 15N-ammonium acetate was incorporated into urinary 15N-nitrate in rats, suggesting that ammonia is a precursor of nitrate. Furthermore, Escherichia coli lipopolysaccharide was found to be a potent stimulus of nitrate excretion (nine-fold increase), due to an increased rate of synthesis. Two other types of experimentally induced inflammatory states - injection of carrageenan and of turpentine - enhanced nitrate synthesis. It is proposed that the pathway of nitrate biosynthesis may be the result of oxidation of reduced nitrogen compounds by oxygen radicals generated by an activated reticuloendothelial system.
 ...
PMID:Mammalian nitrate biochemistry: metabolism and endogenous synthesis. 653 15

Palmerston North (PN) mice, a newly recognized model of systemic lupus erythematosus, were compared with autoimmune hybrid NZB/NZW mice in a study designed to examine spleen cell responsiveness to T-cell and B-cell mitogens. Modest reductions of responses to phytohemagglutinin (PHA) and concanavalin A (Con A) were noted in PN females after 24 weeks of age; these responses were reduced significantly in NZB/NZW females. In contrast, male PN and NZB/NZW mice responded actively to PHA and Con A throughout the first year of life. Responses to lipopolysaccharide were not affected by age or sex. Anti-DNA antibody levels, blood urea nitrogen, and glomerular histology were analyzed to determine if autoantibody production or renal failure correlated with suppressed mitogenic responsiveness. These factors, examined singly and together, were not as important as age. In this system, age and sex did not influence spleen cell responses to mitogens in normal CD-1 mice. Age and sex were of minimal importance in determining responses to T-cell mitogens in the recently defined PN model of autoimmunity. In contrast, age and sex exerted strong influences upon responses to PHA and Con A in the NZB/NZW model of lupus.
 ...
PMID:Responses to T-cell and B-cell mitogens in autoimmune Palmerston North and NZB/NZW mice. 660 3

Prolonged culturing in the laboratory has resulted in the formation of a stable derivative of the smooth Group E bacterial strain, Salmonella anatum A1, that is sensitive to both the R-core-specific bacteriophage Felix 01 and O-polysaccharide-specific bacteriophage epsilon 15. The variant strain, designated S. anatum A1-1, exhibits a normal number of irreversible binding sites for epsilon 15 but the relative quality and/or accessibility of those sites appears to be diminished. Infectious epsilon 15 phage particles are released more rapidly from S. anatum A1-1 than from its parent under acidic pH conditions known to interfere with the phage DNA ejection step. The purified lipopolysaccharide (LPS) of S. anatum A1-1 exhibits a reduced rhamnose/heptose ratio in chemical assays. Fractionation of this LPS on SDS-urea-polyacrylamide gels followed by silver staining reveals a narrower range of O-polysaccharide chain lengths relative to that of the parent (0 to 20 vs. 0 to 40 repeating units, respectively).
 ...
PMID:Evidence for shorter average O-polysaccharide chainlength in the lipopolysaccharide of a bacteriophage Felix 01-sensitive variant of Salmonella anatum A1. 665 58

An extract from the seeds of Persea americana possessed an erythro-agglutinating activity. The agglutinin was devoid of specificity for carbohydrates, but interacted readily with basic proteins or basic polyamino acids. The interaction between the agglutinin and egg-white lysozyme was not inhibited by chaotropic salts, but was sensitive to relatively low concentrations of urea. An affinity chromatographic procedure was developed in an effort to purify the agglutinin. Products from the chromatographic procedure were found not to contain higher specific agglutinating activities than the crude extract. Amino acid acid analyses of the extract showed the presence of relatively high proportions of glutamic and aspartic acids. In addition, the extract contained phosphorus and a visible chromophore. The agglutinin was resistant to detergents and denaturants, and proteases, nucleases, and other enzymes. The results suggest that, as opposed to other plant agglutinins, the active component from Persea is not a protein. Similarly, in contrast to many lectins, the agglutinin from Persea was not mitogenic for mouse lymphocytes. The agglutinin partially inhibited the mitogenesis of lymphocytes when the cells were treated with concanavalin A, or with bacterial lipopolysaccharide.
 ...
PMID:Lectin-like activity from Persea americana. 735 11


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>