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See detailDiagnostic différentiel en cas de présomption de myopathie atypique des équidés : illustration au travers de cas référés à la Faculté de Médecine Vétérinaire de l’Université de Liège au cours du printemps 2003
Votion, Dominique ULg; Delguste, Catherine ULg; Baise, Etienne ULg et al

in Annales de Médecine Vétérinaire (2003), 147

Atypical myopathy is a frequently fatal disease inducing extensive and severe muscular damage, occurring during autumn and spring in grazing horses. The main features of the syndrome are the sudden onset ... [more ▼]

Atypical myopathy is a frequently fatal disease inducing extensive and severe muscular damage, occurring during autumn and spring in grazing horses. The main features of the syndrome are the sudden onset of non pathognomonic symptoms such as weakness, stiffness, sudation, recumbency and when observed, emission of dark urine. Confirmation of the diagnosis is of paramount importance since the disease can be recurrent on limited geographic area. This paper discusses the methodology applied on 7 clinical cases referred with a symptomatology suggestive of atypical myopathy to the Faculty of Veterinary Medicine at Liege University during the spring 2003. Two of those cases were confirmed for atypical myopathy. A presumption of atypical myopathy may be drawn on history and clinical signs. On living animals, the serum concentration of the creatinine phosphokinase enzyme is the most useful biochemical tests as an aid to diagnosis because it confirms the presence of muscle damage. Nevertheless, the definitive diagnosis requires the histological examination of specific muscular samples obtained post-mortem. [less ▲]

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See detailMyopathies atypiques chez les chevaux au pré: une série de cas en Belgique
Delguste, Catherine ULg; Cassart, Dominique ULg; Baise, Etienne ULg et al

in Annales de Médecine Vétérinaire (2002), 146(4, AUG-SEP), 235-247

Atypical myoglobinuria in grazing horses was described in United Kingdom and Germany between 1984 and 1996. Fourteen horses were presented at the University of Liege between November 2000 and April 2001 ... [more ▼]

Atypical myoglobinuria in grazing horses was described in United Kingdom and Germany between 1984 and 1996. Fourteen horses were presented at the University of Liege between November 2000 and April 2001, with a clinical history suggesting atypical myoglobinuria. Lesions were similar to those previously described. All horses were at rest and grazing when they developed clinical signs. Three times, the syndrome killed several horses grazing together. Horses were generally found recumbent, nearly or totally unable to stand up. They were presenting tachycardia, polypnoea, myoglobinuria and died rapidly. When performed, blood analysis revealed severe muscular enzymatic activity rises. Histopathology revealed pulmonary congestion and oedema, and squeletal muscular fibers degeneration, mostly in respiratory and postural muscles. These observations are in accordance with cases of atypical myoglobinuria previously described in UK and Germany. The aetiology of this pathology is still unknown, despite of research attempts. [less ▲]

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See detailCold-Adapted Beta-Galactosidase from the Antarctic Psychrophile Pseudoalteromonas Haloplanktis
Hoyoux, A.; Jennes, I.; Dubois, P. et al

in Applied and Environmental Microbiology (2001), 67(4), 1529-35

The beta-galactosidase from the Antarctic gram-negative bacterium Pseudoalteromonas haloplanktis TAE 79 was purified to homogeneity. The nucleotide sequence and the NH(2)-terminal amino acid sequence of ... [more ▼]

The beta-galactosidase from the Antarctic gram-negative bacterium Pseudoalteromonas haloplanktis TAE 79 was purified to homogeneity. The nucleotide sequence and the NH(2)-terminal amino acid sequence of the purified enzyme indicate that the beta-galactosidase subunit is composed of 1,038 amino acids with a calculated M(r) of 118,068. This beta-galactosidase shares structural properties with Escherichia coli beta-galactosidase (comparable subunit mass, 51% amino sequence identity, conservation of amino acid residues involved in catalysis, similar optimal pH value, and requirement for divalent metal ions) but is characterized by a higher catalytic efficiency on synthetic and natural substrates and by a shift of apparent optimum activity toward low temperatures and lower thermal stability. The enzyme also differs by a higher pI (7.8) and by specific thermodynamic activation parameters. P. haloplanktis beta-galactosidase was expressed in E. coli, and the recombinant enzyme displays properties identical to those of the wild-type enzyme. Heat-induced unfolding monitored by intrinsic fluorescence spectroscopy showed lower melting point values for both P. haloplanktis wild-type and recombinant beta-galactosidase compared to the mesophilic enzyme. Assays of lactose hydrolysis in milk demonstrate that P. haloplanktis beta-galactosidase can outperform the current commercial beta-galactosidase from Kluyveromyces marxianus var. lactis, suggesting that the cold-adapted beta-galactosidase could be used to hydrolyze lactose in dairy products processed in refrigerated plants. [less ▲]

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See detailEnzyme Activity Determination on Macromolecular Substrates by Isothermal Titration Calorimetry: Application to Mesophilic and Psychrophilic Chitinases
Lonhienne, T.; Baise, Etienne ULg; Feller, Georges ULg et al

in Biochimica et Biophysica Acta (2001), 1545(1-2), 349-56

Isothermal titration calorimetry has been applied to the determination of the kinetic parameters of chitinases (EC 3.2.1.14) by monitoring the heat released during the hydrolysis of chitin glycosidic ... [more ▼]

Isothermal titration calorimetry has been applied to the determination of the kinetic parameters of chitinases (EC 3.2.1.14) by monitoring the heat released during the hydrolysis of chitin glycosidic bonds. Experiments were carried out using two different macromolecular substrates: a soluble polymer of N-acetylglucosamine and the insoluble chitin from crab shells. Different experimental temperatures were used in order to compare the thermodependence of the activity of two chitinases from the psychrophile Arthrobacter sp. TAD20 and of chitinase A from the mesophile Serratia marcescens. The method allowed to determine unequivocally the catalytic rate constant k(cat), the activation energy (E(a)) and the thermodynamic activation parameters (DeltaG(#), DeltaH(#), DeltaS(#)) of the chitinolytic reaction on the soluble substrate. The catalytic activity has also been determined on insoluble chitin, which displays an effect of substrate saturation by chitinases. On both substrates, the thermodependence of the activity of the psychrophilic chitinases was lower than that observed with the mesophilic counterpart. [less ▲]

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See detailReceptors as screening tools in the detections of hormones. Applications in the control of meat production
Maghuin-Rogister, Guy ULg; Baise, Etienne ULg; Carpeaux, Rudy et al

in Biotechnologie, Agronomie, Société et Environnement = Biotechnology, Agronomy, Society and Environment [=BASE] (1999), 4(1), 21-22

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See detailCold enzymes : a hot topic
Gerday, Charles ULg; Aittaleb, M.; Arpigny, J. L. et al

in Margesin, R.; Schinner, F. (Eds.) Cold-adapted Organisms : Ecology, Physiology, Enzymology and Molecular Biology (1999)

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See detailPsychrophilic Enzymes: A Thermodynamic Challenge
Gerday, Charles ULg; Aittaleb, Mohamed; Arpigny, Jean Louis et al

in Biochimica et Biophysica Acta (1997), 1342(2), 119-31

Psychrophilic microorganisms, hosts of permanently cold habitats, produce enzymes which are adapted to work at low temperatures. When compared to their mesophilic counterparts, these enzymes display a ... [more ▼]

Psychrophilic microorganisms, hosts of permanently cold habitats, produce enzymes which are adapted to work at low temperatures. When compared to their mesophilic counterparts, these enzymes display a higher catalytic efficiency over a temperature range of roughly 0-30 degrees C and a high thermosensitivity. The molecular characteristics of cold enzymes originating from Antarctic bacteria have been approached through protein modelling and X-ray crystallography. The deduced three-dimensional structures of cold alpha-amylase, beta-lactamase, lipase and subtilisin have been compared to their mesophilic homologs. It appears that the molecular adaptation resides in a weakening of the intramolecular interactions, and in some cases in an increase of the interaction with the solvent, leading to more flexible molecular edifices capable of performing catalysis at a lower energy cost. [less ▲]

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See detailPsychrophiles et thermophiles : un problème d’enzyme
Gerday, Charles ULg; Aittaleb, M.; Arpigny, J. L. et al

in Chimie Nouvelle (1997), 15

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See detailEnzymes from psychrophiles
Feller, Georges ULg; Narinx, Emmanuel; Arpigny, Jean Louis et al

Conference (1996)

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See detailEnzymes from psychrophilic organisms
Feller, Georges ULg; Narinx, E.; Arpigny, J. L. et al

in FEMS Microbiology Reviews (1996), 18(2-3), 189-202

Psychrophilic organisms such as micro-organisms and other ectothermic species living in polar, deep- sea or any constantly low temperature environments, produce enzymes adapted to function at low ... [more ▼]

Psychrophilic organisms such as micro-organisms and other ectothermic species living in polar, deep- sea or any constantly low temperature environments, produce enzymes adapted to function at low temperature. These enzymes are characterized by a high catalytic efficiency at low and moderate temperatures but are rather thermolabile. Due to their high specific activity and their rapid inactivation at temperatures as low as 30 degrees C, they offer, along with the producing micro-organisms, a great potential in biotechnology. The molecular basis of the adaptation of cold cu-amylase, subtilisin, triose phosphate isomerase from Antarctic bacteria and of trypsin from fish living in North Atlantic and in Antarctic sea waters have been studied. The comparison of the 3D structures obtained either by protein modelling or by X-ray crystallography (North Atlantic trypsin) with those of their mesophilic counterparts indicates that the molecular changes tend to increase the flexibility of the structure by a weakening of the intramolecular interactions and by an increase of the interactions with the solvent. For each enzyme, the most appropriate strategy enabling it to accommodate the substrate at a low energy cost is selected. There is a price to pay in terms of thermosensibility because the selective pressure is essentially oriented towards the harmonization of the specific activity with ambient thermal conditions. However, as demonstrated by site-directed mutagenesis experiments carried out on the Antarctic subtilisin, the possibility remains to stabilize the structure of these enzymes without affecting their high catalytic efficiency. [less ▲]

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