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See detailProduction of essential oil by in vitro culture of Anthemis nobilis L. and characterization by GC-MS.
Marlier, M.; Fauconnier, Marie-Laure ULg; Jaziri, M. et al

Poster (1992, September 21)

Detailed reference viewed: 19 (2 ULg)
See detailProduction of four amyloidogenic variants of human lysozyme as inclusion bodies in Escherichia coli
Dumont, Janice ULg; Menzer, Linda ULg; Scarafone, Natacha ULg et al

Poster (2009)

Six variants of human lysozyme (I56T, F57I, W64R, D67H, F57I/T70N and W112R/T70N) are associated with a hereditary non-neuropathic systemic amyloidosis. This disease involved an extra cellular deposition ... [more ▼]

Six variants of human lysozyme (I56T, F57I, W64R, D67H, F57I/T70N and W112R/T70N) are associated with a hereditary non-neuropathic systemic amyloidosis. This disease involved an extra cellular deposition of amyloid fibrils made of lysozyme variants in a wide range of organs such as liver, spleen and kidneys [1]. The characterisation at the molecular level of two variants, I56T and D67H, has shown that these mutations reduce the stability and more particularly the global cooperativity of the protein. Consequently, under physiologically relevant conditions, these variants can transiently populate a partially unfolded state in which the beta-domain and the C-helix are cooperatively unfolded while the rest of the protein remains native like [1]. The formation of intermolecular interactions between the regions that are unfolded in this intermediate state is likely to be a fundamental trigger of the aggregation process that ultimately leads to the formation and deposition of fibrils in tissues. In order to study the effects of the other amyloidogenic mutations on the properties of lysozyme and thus to get more insight in the mechanism of amyloid formation, it is necessary to produce them in large quantities. The D67H, I56T and F57I variants are currently produced in Aspergillus niger; the expression in this organism is, however, time consuming and the yield is very low. The attempts to use alternative systems such as Pichia pastoris [2], Saccharomyces cerevisiae, and Arabidopsis thaliana have not been conclusive so far. In this work, we have produced the four single-point lysozyme variants as inclusion bodies in Escherichia coli and explored the possibility to refold them. [1] Dumoulin & al., (2006) Acc. Chem. Res., 39, 603 - 610 [2] Kumita & al., (2006) FEBS J., 273, 711-720 [less ▲]

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See detailProduction of free radicals and oxygen consumption by primary equine endothelial cells during anoxia-reoxygenation.
de la Rebière de Pouyade, Geoffroy ULg; Salciccia, Alexandra ULg; Ceusters, Justine ULg et al

in Open Biochemistry Journal (The) (2011), 5

The endothelium plays an active role in ischemia/reperfusion injuries. Herein, we report the effect of a single or successive cycles of anoxia/reoxygenation (A/R) on the mitochondrial respiratory function ... [more ▼]

The endothelium plays an active role in ischemia/reperfusion injuries. Herein, we report the effect of a single or successive cycles of anoxia/reoxygenation (A/R) on the mitochondrial respiratory function of equine endothelial cells (cultured from carotids) monitored by high resolution oxymetry, and on their production of reactive oxygen species (ROS). ROS were measured by electron paramagnetic resonance (ESR) using POBN and DMPO spin traps, and by gas chromatography (GC) of ethylene released by ROS-induced alpha-keto-gamma-(methylthio)butyric acid (KMB) oxidation. The oxygen consumption significantly decreased with the number of A/R cycles, and POBN-ESR spectra were specific of adducts formed in the cells from superoxide anion. After a one-hour A/R cycle, high intensity DMPO-ESR spectra were observed and assigned to superoxide anion trapping; the GC results confirmed an important production of ROS compared to normoxic cells. These results show that A/R induces mitochondrial alterations in endothelial cells, and strongly stimulates their oxidative activity as demonstrated by ESR and GC methods. [less ▲]

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See detailProduction of freeze-dried lactic acid bacteria starter culture for cassava fermentation into gari.
Yao, Amenan Anastasie ULg; Dortu, Carine; Egounlety, Moutairu et al

in African Journal of Biotechnology (2009), 8(19), 4996-5004

Sixteen lactic acid bacteria, eight Lactobacillus plantarum, three L. pentosus, 2 Weissella paramesenteroides, two L. fermemtum and one Leuconostoc mesenteroides ssp. mesenteroides were previously ... [more ▼]

Sixteen lactic acid bacteria, eight Lactobacillus plantarum, three L. pentosus, 2 Weissella paramesenteroides, two L. fermemtum and one Leuconostoc mesenteroides ssp. mesenteroides were previously isolated from cassava fermentation and selected on the basis of their biochemical properties with a view to selecting appropriate starter cultures during cassava fermentation for gari production. In this study, the potential of these pre-selected strains as suitable freeze-dried cultures was evaluated. Their ability to tolerate the freeze-drying process was assessed by dehydration in a glycerol solution of increasing concentration, followed by staining with two fluorescent markers: rhodamine 123 and propydium iodide. Twelve strains that recovered more than 50% of their population value after visualisation on an epi-fluorescent microscope were produced in a bioreactor and freeze-dried. The technological characteristics identified after the freeze-drying process, were a high cell concentration or high survival rate. The ability of the freeze-dried strains to recover their acidification activity was evaluated through the determination of the pH, titratable acidity (% lactic acid/g Dry Weight) and cell count over 24 h on MRS broth. Ultimately, the strains L. plantarum VE36, G2/25, L. fermentum G2/10 and W. paramesenteroides LC11 were selected to be developed as freeze-dried starter cultures for gari production. [less ▲]

Detailed reference viewed: 87 (11 ULg)
See detailProduction of glycerol by immobilized Saccharomyces cerevisiae in stirred bioreactor.
Destain, Jacqueline ULg; Renault, M.; Rikir, R. et al

Poster (1990, July)

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See detailProduction of heavy clusters (up to A=10) by coalescence during the intranuclear cascade phase of spallation reactions
Cugnon, Joseph ULg; Boudard, A; David, J-C et al

in J. Phys.: Conf. Ser. (2011), 312

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See detailProduction of heavy clusters (up to A=10) by coalescence during the intranuclear cascade phase of spallation reactions
Cugnon, Joseph ULg; Boudard, A; David, J-C et al

in J. Phys: Conf. Ser. (2011), 312

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See detailProduction of hemicellulase by Penicillium canescens 10-10C. Arch. Int. Phys. Bioch., 101, B1-B00.
Fonder, C.; Rikir, R.; Kvesitadze, G. et al

in Archives Internationales de Physiologie et de Biochimie (1993), 101(B1-B100),

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See detailProduction Of Hen Egg Yolk Immunoglobulins Simultaneously Directed Against Salmonella Enteritidis And Salmonella Typhimurium In The Same Egg Yolk
Chalghoumi, Raja ULg; Thewis, André ULg; Portetelle, Daniel ULg et al

in Poultry Science (2008), 87(1), 32-40

The present study was an attempt to raise hen egg yolk Ig (IgY) simultaneously directed against Salmonella Enteritidis (SE) and Salmonella Typhimurium (ST) in the same egg yolk. The immunopotentiating ... [more ▼]

The present study was an attempt to raise hen egg yolk Ig (IgY) simultaneously directed against Salmonella Enteritidis (SE) and Salmonella Typhimurium (ST) in the same egg yolk. The immunopotentiating effect of 2 different adjuvants—Freund’s adjuvants (FA) and immunostimulating complexes matrix (IM)—on antibody response was also evaluated. Bacterial outer membrane proteins (OMP) were selected as target antigens. The ISA Brown hens, specific-Salmonella spp.-free status, divided into 6 groups were intramuscularly injected with a monocompound antigen preparation: SE-OMP (treatment SEFA or SE-IM) or ST-OMP (treatment ST-FA or ST-IM), or a combined antigen preparation: ¹⁄₂ SE-OMP and ¹⁄₂ STOMP (treatment SEST-FA or SEST-IM). Titers of antibodies in yolk were evaluated biweekly with ELISA. There was no antigen × adjuvant interaction on antibody titers. Anti-SE IgY titers in hens that received treatment SESTFA or SEST-IM were statistically similar (P > 0.05) as compared with those obtained from hens immunized with treatment SE-FA or SE-IM. Anti-ST IgY titers in hens immunized with treatment SEST-FA or SEST-IM were slightly lower than those of hens that received treatment ST-FA or ST-IM. The cross-reactivity of anti-SE IgY, induced by treatment SE-FA or SE-IM, with ST-OMP antigen and that of anti-ST IgY, induced by ST-FA or ST-IM, with SE-OMP antigen were arbitrarily assessed on d 43 and 155 by ELISA. The average cross-reactivity of anti-SE IgY with ST-OMP antigen was 71.7%. The average cross-reactivity of anti-ST IgY with SE-OMP antigen was 78.8%. In FA groups, antibody titers were found higher (P < 0.05) than those in IM groups. Furthermore, no extensive lesions or clinical abnormalities were detected in hens injected with FA. These findings showed the opportunity to raise IgY antibody against 2 Salmonella serovars in the same yolk and that FA was more efficient than IM in mediating antibody response. [less ▲]

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See detailProduction of heterobispecific monoclonal antibodies by mouse hybrid hybridomas (quadromas)
Cloes, Jean-Michel; Herens, Christian ULg; Nys, Monique ULg et al

in Archives Internationales de Physiologie, de Biochimie et de Biophysique (1988), 96

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See detailProduction of high-gossypol cotton plants with low-gossypol seed from trispecific hybrids including gossypium sturtianum willis
Mergeai, Guy ULg; Baudoin, Jean-Pierre ULg; Vroh Bi, I

in proceedings of the World Cotton Research Conference 2 (1998)

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See detailProduction of interferon gamma by peripheral blood mononuclear cells from normal subjects and from patients with rheumatoid arthritis
Reuter, A.; Bernier, J.; Vrindts-Gevaert, Y. et al

in Clinical and Experimental Rheumatology (1988), 6(4, Oct-Dec), 347-354

A radioimmunoassay for human interferon gamma (IFN-gamma) has been carried out using a recombinant glycosylated interferon (Hu IFN-gamma) as tracer, the N.I.H. reference preparation (Gg 23-901-530) and a ... [more ▼]

A radioimmunoassay for human interferon gamma (IFN-gamma) has been carried out using a recombinant glycosylated interferon (Hu IFN-gamma) as tracer, the N.I.H. reference preparation (Gg 23-901-530) and a polyclonal rabbit antiserum. The assay is highly specific for IFN-gamma: there is no cross-reaction either with interferons alpha and beta, Interleukins 1 and 2, tumor necrosis factor alpha and beta or with various brain peptides. The sequential saturation procedure allowed a sensitivity of 0.4 U/ml with intra and between assay coefficients of variation less than 8 and 12%, respectively. The in-vitro production of IFN-gamma by peripheral blood mononuclear cells (P.B.M.C.) was also measured. In unstimulated cultures, IFN-gamma production remained undetectable, i.e. below the 0.4 U/ml sensitivity level. After stimulation of P.B.M.C. from normal subjects with increasing amounts of PHA, both the 3H-thymidine incorporation and IFN-gamma release followed bell-shaped curves. There was no significant difference of 3H-thymidine incorporation between PHA stimulated cultures (0.2 and 2.5 ug/ml) from normal subjects (36 cases) and those with active (16 cases) or non-active (14 cases) rheumatoid arthritis. At two PHA concentrations of 0.2 and 2.5 ug/ml, mononuclear cells from patients with active disease produced significantly less IFN-gamma than those from either controls or cases with non-active disease. [less ▲]

Detailed reference viewed: 11 (0 ULg)