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)

The outer membrane complex of Rochalimaea quintana was isolated by use of ethylene-eiaminetetraacetate and was compared biochemically and biologically both with lipopolysaccharide (LPS) isolated by phenol-water extraction of whole organisms and with lipids isolated by chloroform-methanol extractions of the phenol-water insoluble residues. The outer membrane consisted of protein and LPS components, as distinguished by precipitin tests with sera from patients with trench fever or tests with hyperimmune animal sera. The outer membrane protein component, but not LPS, also reacted with sera from infections with Rickettsia tsutsugamushi. The LPS contained 2-keto-3-deoxy-octonate and heptose. The outer membrane and phenol-extracted LPS were reactive in the chick embryo lethality test, limulus assay, and complement activation. Outer-membrane activity was confined to the LPS component. The lipid extracts were reactive in chick embryo lethality and limulus assays, but did not activate complement.
 ...
PMID:Immunochemical and biological properties of the outer membrane-associated lipopolysaccharide and protein of Rochalimaea quintana. 676 14

We assessed the ability of a solid-phase radioimmunoassay, modified to allow antigen detection in serum, to detect circulating antigens in granulocytopenic rabbits with Pseudomonas aeruginosa bacteremia. In vitro experiments with Pseudomonas lipopolysaccharide indicated that treatment of serum-lipopolysaccharide mixtures with heat, chloroform, or heparin improved the sensitivity for detecting lipopolysaccharide 8- to 16-fold. Chloroform treatment permitted antigen detection in serum or plasma of bacteremic rabbits in which antigen could be detected poorly or not at all in untreated specimens. However, chloroform-treated specimens occasionally caused dissolution of plastic tubes, resulting in nonspecific binding of 125I-labeled anti-Pseudomonas immunoglobulin G. Heating sera at 56 degree C for 30 min improved antigen detection both in both in lipopolysaccharide-serum mixtures and in bacteremic rabbits. Antigen was detected in the heated serum or plasma of 20% of 20 culture-positive granulocytopenic rabbits, none of 15 culture-negative granulocytopenic rabbits, and none of 38 normal rabbits. Antigen was detected in none of 15 rabbits with 2 to 300 colony-forming units of P. aeruginosa per ml of blood and in 4 of 5 rabbits with > 10(3) colony-forming units per ml. We conclude that circulating antigens are present in the blood of rabbits with high-level P. aeruginosa bacteremia and that these antigens can be detected by solid-phase radioimmunoassay. Further improvements in assay sensitivity will be required to detect antigens, if present, in animals with lower levels of P. aeruginosa bacteremia.
 ...
PMID:Detection of Pseudomonas aeruginosa antigenemia in granulocytopenic rabbits by radiommunoassay. 677 8

Mild hydrolysis of Haemophilus influenzae type a lipopolysaccharide by ion exchangers yielded a lipid A extracted by chloroform. It contained phosphorus, glucosamine, and fatty acids. Myristic, palmitic, 3-hydroxymyristic, and oleic acids and two other unidentified long-chain fatty acids were found. The free lipid A was not toxic for mice at doses of up to 50 mg/kg and did not provoke a Shwartzman reaction. The Limulus test activity was positive up to 10(-12) g/ml, but the pyrogenicity in rabbits was lower than with the original lipopolysaccharide. However, the lipid A did induced a mitogenic response and polyclonal B-cell activation in mouse spleen cell cultures. Complexing lipid A with bovine serum albumin gave a nontoxic preparation which lost these immunological activities. Immunochemical studies showed that the major reactive determinants of this lipid-protein complex were altered after such a linkage. Consequently, the nontoxic and mitogenic lipid A isolated from H. influenzae type a did not exhibit all of the classical activities of lipid A preparations.
 ...
PMID:Characteristics of a lipid preparation (lipid A) from Haemophilus influenzae type a lipopolysaccharide. 679 Apr 42

Biochemical measures have provided insight into the biomass and community structure of sedimentary microbiota without the requirement of selection by growth or quantitative removal from the sediment grains. This study used the assay of the hydroxy fatty acids released from the lipid A of the lipopolysaccharide in sediments to provide an estimate of the gram-negative bacteria. The method was sensitive to picomolar amounts of hydroxy fatty acids. The recovery of lipopolysaccharide hydroxy fatty acids from organisms added to sediments was quantitative. The lipids were extracted from the sediments with single-phase chloroform-methanol extraction. The lipid-extraction residue was hydrolyzed in 1 N HCl, and the hydroxy fatty acids of the lipopolysaccharide were recovered in chloroform for analysis by gas-liquid chromatography. This method proved to be about fivefold more sensitive than the classical phenol-water or trichloroacetic acid methods when applied to marine sediments. By examination of the patterns of hydroxy fatty acids, it was also possible to help define the community structure of the sedimentary gram-negative bacteria.
 ...
PMID:Sensitive assay, based on hydroxy fatty acids from lipopolysaccharide lipid A, for Gram-negative bacteria in sediments. 681 12

Mild hydrolysis of Haemophilus influenzae type a lipopolysaccharide by ion exchangers in the presence of chloroform, to remove the lipid moiety, yielded a nontoxic and immunogenic polysaccharide fraction. This polysaccharide selectively triggered murine B lymphocytes in vitro: (i) it induced enhancement of thymidine incorporation and stimulated antibody secretion in cultures of normal and nude mouse spleen cells; (ii) it did not stimulate splenic T lymphocytes; (iii) the activation of B lymphocytes was not absolutely dependent on the presence of macrophages. Sepharose 4B gel filtration showed that this polysaccharide consisted at least of two fractions: PS I (molecular weight [MW] 10(6)) and PS II (MW 10(4)). Only PS I was found to act as a polyclonal B cell activator. EDTA treatment dissociated the polysaccharide into PS III (MW 10(6)) and PS IV (MW 10(4)), which was not reassembled after the addition of 0.02 M CaCl2. Both fractions PS III and PS IV were unable to stimulate B lymphocytes. The immunological active fraction of H. influenzae polysaccharide is PS I. This fraction consists of a high-molecular-weight group (10(6)) and an association of 10(4)-MW aggregated units.
 ...
PMID:In vitro immunological activities of the polysaccharide fraction from Haemophilus influenzae type a endotoxin. 697 13

A sequential extraction procedure was used to provide 3 endotoxin fractions from Pasteurella haemolytica with distinct biological and solubility properties. After acetone dessication, extraction with phenol, chloroform, and petroleum ether (2:5:8) provided a fraction designated rough lipopolysaccharide (LPS). Subsequent extraction of the cells with 45% phenol at 68 C yielded a fraction designated smooth LPS, which was further divided into smooth precipitate and smooth supernatant, based on sedimentation at 105,000 x g for 4 hours. Yields of the 3 fractions were 1.5%, 3%, and 5.5% of the dry weight of the cells. The polysaccharide moieties of the rough LPS amd smooth precipitate fractions were obtained by partial acid hydrolysis followed by chloroform extraction. Biological activities of all 5 fractions were compared with activities of standard LPS fractions from Serratia marcescens and Salmonella typhimurium. Results of chicken embryo lethality, the local Shwartzman's phenomenon, nonspecific resistance enhancement ot challenge exposure by S typhimurium pyrogenicity, and the Limulus amebocyte lysate assay were reported.
 ...
PMID:Purification and biological characterizationof endotoxin fractions from Pasteruella haemolytica. 704 5

The lipopolysaccharide of Acinetobacter calcoaceticus NCTC 10305 (London) was obtained by a modified phenol/chloroform/light petroleum method from the bacterial cells and from the culture medium in yields of 1.6% and 2.2% respectively (based on the bacterial dry weight). On chemical analysis, both preparations proved to be identical. The lipopolysaccharide obtained from the cells was purified by repeated ultracentrifugation, electrodialysis, and precipitation with sodium chloride. It was free of nucleic acids, proteins, and glycans. In the analytical ultracentrifuge, the triethylamine and sodium salt forms of the lipopolysaccharide showed a s20 value of 8.9 S and 51 S, respectively. The lipopolysaccharide consisted of glucosamine, 3-deoxy-D-manno-octulosonic acid, D-glucose, fatty acids, and phosphate in a molar ratio of 2:1:7:6:4. The fatty acids were predominantly lauric acid, 2-hydroxy, and 3-hydroxylauric acid in a molar ratio of 1:1:2. Only 3-hydroxylauric acid was found in amide linkage. On mild acid hydrolysis of the lipopolysaccharide, 65% lipid A were obtained, to which glucosamine was retained quantitatively. It still contained 50% of the original glucose, while one third (15%) of the liberated glucose was in monomeric form.
 ...
PMID:Isolation, purification, and chemical analysis of the lipopolysaccharide and lipid A of Acinetobacter calcoaceticus NCTC 10305. 706 May 73

Our previous finding that the cerebral proteolipid could inactivate the pyrogenicity of lipopolysaccharide (LPS) in vitro was also studied by Sephadex LH-20 column chromatography and the following results were obtained. When rabbit cerebral proteolipid was chromatographed, two main protein peaks were obtained. One appeared in the chloroform (C)/methanol (M) 6:1 and the other C/M 4:1 effluent, designated as fraction IV and fraction V, respectively. When the incubation mixture of proteolipid and LPS was chromatographed, a new protein peak appeared in the C effluent. The new protein peak was suggested to be a complex of proteolipid protein and LPS, because pyrogenicity could be detected in the protein fractions only after treatment with 2% SDS. Fraction V but not fraction IV inactivated the pyrogenicity of LPS in vitro. By re-chromatography of the incubation mixture of fraction V and LPS, a complex of protein and LPS was also eluted in the C effluent. On the other hand, by rechromatography of the incubation mixture of fraction IV and LPS, such a complex was not detected in the C effluent. The present results suggest that the proteolipid apoprotein eluted in the C/M 4:1 effluent on a Sephadex LH-20 column plays an important role in the inactivation of the pyrogenicity of LPS.
 ...
PMID:Interactions between bacterial pyrogen and proteolipid extracted fom the cerebrum (II). 731 Nov 54

Smooth, rough, and neutral forms of lipopolysaccharide (LPS) from Pseudomonas aeruginosa were used to assess the appropriate conditions for effective enzyme-linked immunosorbent assay (ELISA) of LPS. Each of these forms of well-defined LPS was tested for the efficiency of antigen coating by various methods as well as to identify an appropriate type of microtiter plate to use. For smooth LPS, the standard carbonate-bicarbonate buffer method was as efficient as the other sensitivity-enhancing plate-coating methods compared. The rough LPS, which has an overall hydrophobic characteristic, was shown to adhere effectively, regardless of the coating method used, to only one type of microtiter plate, CovaLink. This type of plate has secondary amine groups attached on its polystyrene surface by carbon chain spacers, which likely favors hydrophobic interactions between the rough LPS and the well surfaces. Dehydration methods were effective for coating microtiter plates with the neutral LPS examined, which is composed predominantly of a D-rhamnan. For the two dehydration procedures, LPS suspended in water or the organic solvent chloroform-ethanol was added directly to the wells, and the solvent was allowed to dehydrate or evaporate overnight. Precoating of plates with either polymyxin or poly-L-lysine did not give any major improvement in coating with the various forms of LPS. The possibility of using proteinase K- and sodium dodecyl sulfate-treated LPS preparations for ELISAs was also investigated. Smooth LPS prepared by this method was as effective in ELISA as LPS prepared by the hot water-phenol method, while the rough and neutral LPSs prepared this way were not satisfactory for ELISA.
 ...
PMID:Appropriate coating methods and other conditions for enzyme-linked immunosorbent assay of smooth, rough, and neutral lipopolysaccharides of Pseudomonas aeruginosa. 749 23

The lipopolysaccharide (LPS) of the Pseudomonas aeruginosa serotype 06 rough-type mutant A28 was isolated by a modified phenol-chloroform-petroleum ether extraction method. Deoxycholate-polyacrylamide gel electrophoresis indicated a single band with mobility similar to that of the complete core region of the wild-type parent serotype 06 (International Antigenic Typing Scheme) strain. Compositional analysis of the LPS indicated that the core oligosaccharide was composed of D-glucose (three units), L-rhamnose (one unit), 2-amino-2-deoxy-D-galactose (one unit), L-glycero-D-manno-heptose (two units), 3-deoxy-D-manno-octulosonic acid (two units), L-alanine (one unit), and phosphate (two units). Under the mild conditions of hydrolysis with methanolic hydrogen chloride, a 7-O-carbamoyl substituent was observed on the second heptose residue. The glycan structure of the LPS was determined by employing one- and two-dimensional nuclear magnetic resonance spectroscopy and mass spectrometry-based methods with a backbone oligosaccharide that was obtained from the LPS by deacylation, dephosphorylation, and reduction of the terminal glucosamine. On the basis of the results of the present study and our earlier work with the P. aeruginosa 06-derived core-defective mutant R5 (H. Masoud, E. Altman, J. C. Richards, and J. S. Lam, Biochemistry, 33:10568-10578, 1994), a structural model for the complete core oligosaccharide is proposed.
 ...
PMID:Structural elucidation of the lipopolysaccharide core region of the O-chain-deficient mutant strain A28 from Pseudomonas aeruginosa serotype 06 (International Antigenic Typing Scheme). 759 59


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