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See detailPurification and properties of the replicative form of Semliki Virus RNA
Osterrieth, P. M.; Rentier-Delrue, Françoise ULg; Calberg-Bacq, C. M. et al

in Hoppe Seyler's Zeitschrift für Physiologische Chemie (1974)

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See detailPurification de la [beta]-(1-4)-N-acétylhexosaminidase sécrétée par Streptomyces albus G et active sur les parois de Micrococus lysodeikticus
Dierickx, L.; Ghuysen, Jean-Marie ULg

in Biochimica et Biophysica Acta (1962), 58

The N-acetylhexosaminidase (referred as Str) secreted by Streptomyces albus G. has been purified by zone electrophoresis. It is slightly less basic than egg-white lysozyme. Its isoelectric point is close ... [more ▼]

The N-acetylhexosaminidase (referred as Str) secreted by Streptomyces albus G. has been purified by zone electrophoresis. It is slightly less basic than egg-white lysozyme. Its isoelectric point is close to pH 10.3. It has no action on the [alpha]- and [beta]-phenylglycosides of N-acetylglucosamine and on the disaccharides [beta]-(1-4)-di-N-acetylglucosamine (di-N-acetylchitobiose) and [beta]-(1-6)-N-acetylglucosaminyl-N-acetylmuramic acid but it splits the tetrasaccharide [beta]-(1-4)-tetra-N-acetylglucosamine(tetra-N-acetylchitotetraose) in di-N-acetylchitobiose. Contrary to lysozyme, it does not split the tetrasaccharide O-[beta]-N-acetylglucosaminyl-(1-6)-O-[beta]-N-acetylmuraminyl-(1-4)-O-[beta]-N-acetylglucosaminyl-(1-6)-[beta]-N-acetylmuramic acid in disaccharide by hydrolyzing the [beta](1-4) linkage. In those conditions the disaccharide liberated, as well as the tetrasaccharide, from Microccus lysodeikticus cell walls after incubation with the N-acetylhexosaminidase Str, can not be put down to a further digestion of some tetrasaccharidic fragments. A chitobiase only active on the [beta]-phenyl-glycoside of N-acetylglucosamine and on the di-N-acetylchitobiose is also present in contentrated culture filtrates. It is a protein acid at pH 6.6. [less ▲]

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See detailPurification de protéines associées à la gestation (PAG) chez le porc
Dethier, M.; Melo de Sousa, Noelita ULg; Balci, S. et al

Poster (2009)

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See detailPurification et caractérisation de la conductine au sodium
Grandfils, Christian ULg

Master's dissertation (1984)

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See detailPurification of a novel dehydrogenase : a vanillin : NAD(P) oxidoreductase.
Bare, G.; Moukil, M. A.; Swiatkowski, T. et al

Poster (1995, February)

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See detailPurification of active matrix metalloproteinase catalytic domains and its use for screening of specific stromelysin-3 inhibitors.
Kannan, R.; Ruff, M.; Kochins, J. G. et al

in Protein Expression & Purification (1999), 16

The matrix metalloproteinase (MMP) stromelysin-3 (ST3) has been shown to be involved in malignant tumor progression and therefore represents an attractive therapeutical target. In order to screen for ST3 ... [more ▼]

The matrix metalloproteinase (MMP) stromelysin-3 (ST3) has been shown to be involved in malignant tumor progression and therefore represents an attractive therapeutical target. In order to screen for ST3 synthetic inhibitors, we have produced and purified the catalytic domain of ST3, matrilysin, stromelysin-2, and membrane type-1 MMP from inclusion bodies in a bacterial system. Our strategy allowed the purification of MMPs directly in the active form, thereby avoidingin vitroactivation. A total of 140,000 synthetic compounds from the Bristol-Myers Pharmaceutical Research Institute chemical deck were tested, using a substrate-based colorimetric enzymatic assay, in which ST3 activity was evaluated through its ability to cleave and inactivate α-1 proteinase inhibitor. One ST3 inhibitor belonging to the cephalosporin family of antibiotics was thereby identified. [less ▲]

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See detailPurification Of Antifungal Lipopeptides By Reversed-Phase High-Performance Liquid-Chromatography
Razafindralambo, Hary ULg; Paquot, Michel ULg; Hbid, Choukri et al

in Journal of Chromatography. A (1993), 639(1), 81-85

A rapid procedure for the purification of antifungal lipopeptides from Bacillus subtilis, a potential agent for biocontrol of plant diseases, was tested. It consists of a solid-phase extraction on C18 gel ... [more ▼]

A rapid procedure for the purification of antifungal lipopeptides from Bacillus subtilis, a potential agent for biocontrol of plant diseases, was tested. It consists of a solid-phase extraction on C18 gel followed by reversed-phase chromatography using a biocompatible PepRPC HR 515 column with a pharmacia fast protein liquid chromatographic system. This is a very effective method for isolating and fractionating iturin A and surfactin, two lipopeptides of different nature, co-produced by Bacillus subtilis strain S499. The presence of homologous lipopeptides was easily detected. [less ▲]

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See detailPurification of antifungal lipopeptides by RPC with FPLC system.
Razafindralambo, Hary ULg; Hbid, Ch.; Jacques, Ph. et al

Poster (1992, October)

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See detailPurification of bovine leukemia virus gp70 and bovine leukemia virus p24. Detection by radioimmunoassay of antibodies directed against these antigens.
Portetelle, Daniel ULg; Mammerickx, Marc; Bex, Françoise et al

in Burny, Arsène (Ed.) Bovine leukosis: various methods of molecular virology (1977)

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See detailPurification of high molecular weight bacteriocin.
Jabrane, A.; Compère, P.; Thonart, Philippe ULg

Poster (1995, February)

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See detailPurification of mouse monoclonal antibodies from ascitic fluid by DEAE Affi-gel Blue chromatography.
Bruck, Claudine; Drebin, J.; Glineur, C. et al

in Langone, J.; Van Vunakis, H. (Eds.) Methods in Enzymology-Immunochemical Techniques - Part J (1986)

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See detailPurification of myeloperoxidase from equine polymorphonuclear leucocytes.
Mathy, Marianne ULg; Bourgeois, E.; Grulke, Sigrid ULg et al

in Canadian Journal of Veterinary Research = Revue Canadienne de Recherche Vétérinaire (1998), 62(2), 127-32

Increases of plasma concentrations of neutrophil myeloperoxidase (MPO) can be used as markers of polymorphonuclear leucocytes (PMN) activation in pathological situations (sepsis, acute lung injury, acute ... [more ▼]

Increases of plasma concentrations of neutrophil myeloperoxidase (MPO) can be used as markers of polymorphonuclear leucocytes (PMN) activation in pathological situations (sepsis, acute lung injury, acute inflammation). To develop an assay for measurement of plasma MPO in horses during the above-mentioned infectious and inflammatory conditions, MPO was purified from equine PMN isolated from blood anticoagulated with citrate. PMN were extracted in a saline milieu (0.2 M Na acetate, 1 M NaCl, pH 4.7) to eliminate most of cellular proteins. Pellets were then extracted in the same buffer containing cationic detergent (1% cetyltrimethyl ammonium bromide). The supernatant was further purified by ion exchange chromatography (Hiload S Sepharose HP column 0.5 x 26 cm, equilibrated with 25 mM Na acetate, 0.2 M NaCl, pH 4.7) with a NaCl gradient (until 1 M). Most of the peroxidase activity of MPO (spectrophotometrically measured by the oxidation of orthodianisidine by hydrogen peroxide) was eluted at 0.65 M NaCl. MPO was further purified by gel filtration chromatography (Sephacryl S 200 column 2.6 x 42 cm with 25 mM Na acetate, 0.2 M NaCl, pH 4.7). MPO (specific activity: 74.3 U/mg) was obtained with a yield of 30% from the detergent extraction supernatant. Electrophoresis (non-reducing conditions) showed 3 bands identified, by comparison with human MPO, (i) the mature tetrameric enzyme (150 kDa) with 2 light and 2 heavy subunits, (ii) the precursor form (88 kDa) and (iii) a form of the heavy subunit without the prosthetic heme group (40 kDa). The mature enzyme and its precursor were glycosylated and possessed peroxidase activity. Equine MPO showed strong similarities with human and bovine MPO, with an absorption peak at 430 nm (Soret peak) characteristic of ferrimyeloperoxidase. Enzymatic activity was pH dependent (optimal value at pH 5.5). [less ▲]

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See detailPurification of pectin from apple pomace juice by using sodium caseinate and characterisation of their binding by isothermal titration calorimetry
Happi Emaga, Thomas; Garna, Haikel; Paquot, Michel ULg et al

in Food Hydrocolloids (2012), 29

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See detailPurification of pregnancy-associated glycoproteins from late-pregnancy Bubalus bubalis placentas and development of a radioimmunoassay for pregnancy diagnosis in water buffalo females.
Barbato, Olimpia; Melo de Sousa, Noelita ULg; Barile, Vittoria Lucia et al

in BMC Veterinary Research (2013), 9

BACKGROUND: Pregnancy-associated glycoproteins (PAGs) were first described as placental antigens present in the blood serum of the mother soon after implantation. Here, we describe the purification of ... [more ▼]

BACKGROUND: Pregnancy-associated glycoproteins (PAGs) were first described as placental antigens present in the blood serum of the mother soon after implantation. Here, we describe the purification of several pregnancy-associated glycoproteins from water buffalo placenta (wbPAGs). A specific radioimmunoassay (RIA) was developed for early pregnancy diagnosis in buffalo species. RESULTS: Amino-terminal microsequencing of immunoreactive placental proteins allowed the identification of eleven wbPAGs sequences [Swiss-Prot accession numbers: P86369 to P86379]. Three polyclonal antisera (AS#858, AS#859 and AS#860) were raised in rabbits against distinct wbPAG fractions. A new RIA (RIA-860) was developed and used to distinguish between pregnant (n = 33) and non-pregnant (n = 26) water buffalo females. CONCLUSIONS: Our results confirmed the multiplicity of PAG expression in buffalo placenta. In addition, the RIA-860 system was shown to be sensitive, linear, reproducible, accurate and specific in measuring PAG concentrations in buffalo plasma samples from Day 37 of gestation onwards. [less ▲]

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See detailPurification of Progelatinases A and B by Continuous-Elution Electrophoresis
Remacle, A. G.; Baramova, E. N.; Weidle, U. H. et al

in Protein Expression & Purification (1995), 6(4), 417-22

Progelatinases A and B were purified from HT1080-conditioned culture medium using a continuous-elution electrophoresis. Initially cell culture medium was ammonium sulfate precipitated. The concentrated ... [more ▼]

Progelatinases A and B were purified from HT1080-conditioned culture medium using a continuous-elution electrophoresis. Initially cell culture medium was ammonium sulfate precipitated. The concentrated proteins were affinity chromatographed on gelatin-Sepharose column. The bound gelatinases were eluted with electrophoresis sample buffer and subjected to continuous-elution electrophoresis. In a single run, under the standardized working conditions, the obtained fractions contained four purified enzymes--progelatinase A (M(r) 72,000), its activated forms (M(r) 62,000 and M(r) 59,000), and progelatinase B (M(r) 92,000). Moreover, the continuous-elution electrophoresis allowed the enzymes separation from their respective inhibitors--TIMP-1 (M(r) 28,500) and TIMP-2 (M(r) 21,000). The purified progelatinases A and B demonstrated high specific activities (150-200 U/micrograms). [less ▲]

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See detailPurification of soybean lipoxygenase isoenzyme-1
Fauconnier, Marie-Laure ULg; Marbehan, J.; Blecker, Christophe ULg et al

Poster (1995, February 20)

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See detailPurification of soybean lipoxygenase isoenzyme-1 and characterization of its inhibition by 13-hydroperoxides.
Fauconnier, Marie-Laure ULg; Marlier, M.

in Grasas y Aceites (1996), 47(4), 242-246

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See detailPurification of the recombinant beta2 toxin (CPB2) from an enterotoxaemic bovine Clostridium perfringens strain and production of a specific immune serum
Lebrun, Maud; Filée, Patrice ULg; Galleni, Moreno ULg et al

in Protein Expression & Purification (2007), 55(1), 119-131

Overgrowth of Clostridium perfringens clones with production of one or more of its toxin(s) results in diverse digestive and systemic pathologies in human and animals, such as cattle enterotoxaemia. The ... [more ▼]

Overgrowth of Clostridium perfringens clones with production of one or more of its toxin(s) results in diverse digestive and systemic pathologies in human and animals, such as cattle enterotoxaemia. The so-called beta2 toxin (CPB2) is the most recently described major toxin produced by C perfringens. In this study, the cpb2 ORF (cpb2FM) from a cattle C perfringens-associated enterotoxaemia was cloned and sequenced. The cpb2FM and its deduced nucleotide sequence clearly corresponded to the epb2 allele considered as "consensus" and not to "atypical" allele, despite its "non-porcine" origin. Expression assays of the recombinant toxin CPB2FM were performed in Escherichia coli and Bacillus subtilis with the expression vector pBLTS72, and by genomic integration by double recombination in B. subtilis. Highest level of production was obtained with the expression vector in B. subtilis 168 strain. The recombinant CPB2FM protein was purified and a specific rabbit polyclonal antiserum was produced. Polyclonal antibodies could detect CPB2 production in supernatants of C. perfringens from enterotoxaemic cattle. (C) 2007 Elsevier Inc. All rights reserved. [less ▲]

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See detailA purification procedure of the tetrodotoxin binding component coming from the electroplaxes of E. electricus.
Dandrifosse, Guy ULg; Grandfils, Christian ULg; Bettendorff, Lucien et al

in Changeux, J.P.; Maelicke, A; Neumann, E (Eds.) Molecular Basis of Nerve Activity (1984)

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