L'esprit blanc / par Jules-B. d'Auriac [et Gustave Aimard]

Collection : Les drames du Nouveau-Monde

Mesure du rapport d'embranchement de B → π⁰lv et extraction de l'élément |V[indice]u[indice]b| de la matrice CKM à l'expérience BABAR à l'aide de la technique des étiquettes B → D⁽*⁾lv

Thèse diffusée initialement dans le cadre d'un projet pilote des Presses de l'Université de Montréal/Centre d'édition numérique UdeM (1997-2008) avec l'autorisation de l'auteur.

La confusión b-d en escolares disléxicos.

Resumen basado en el del autor

Purificação e caracterização parcial de uma B-D glicosidade de Artemia franciscana com ação sobre celobiose e lactose

-D-glucosidase (EC 3.2.1.21) is one of the most interesting glycosidases, especially for hydrolysis cellobiose releasing glucose, is last step degradation of cellulose. This function makes the -D-glucosidase is of great interest as a versatile industrial biocatalyst, being critical to various bio-treatment / biorefinery processes, such as bioethanol production. Hen in the report, a -D-glucosidase was extracts from protein extracted of the invertebrate marine Artemia franciscana was purified and characterized with a combination of precipitation with ammonium sulfate (0 - 30%, 30 to 50%, 50 to 80%), the fraction saturated in the range of 30 to 50% (called F-II) was applied in a molecular exclusion chromatography, in Sephacryl S-200, the fractions corresponding to the first peak of activity of -D-glucosidase were gathered and applied in a chromatography of ion exchange in Mono Q; the third peak this protein obtained chromatography, which coincides with the peak of activity of -D-glucosidase was held and applied in a gel filtration chromatography Superose 12 where the first peak protein, which has activity of -D-glucosidase was rechromatography on Superose 12. This enzyme is probably multimerica, consisting of three subunit molecular mass of 52.7 kDa (determined by SDS-PAGE) with native molecular mass of 157 kDa (determined by gel filtration chromatography on Superose 12 under the system FPLC). The enzyme was purified 44.09 times with a recovery of 1.01%. Using up p-nitrophenyl-β-D-glucopiranoside as substrate obtained a Km apparent of 0.229 mM and a Vmax of 1.109 mM.60min-1.mL-1mM. The optimum pH and optimum temperature of catalysis of the synthetic substrate were 5.0 and 45 °C, respectively. The activity of the -D-glucosidase was strongly, inhibited by silver nitrate and N- etylmaleimide, this inhibition indicates the involvement of radical sulfidrila the hydrolysis of synthetic substrate. The -D-glucosidase of Artemia franciscana presented degradativa action on celobiose, lactose and on the synthetic substrate -nitrophenyl-β-D-glucopiranoside indicating potential use of this enzyme in the industry mainly for the production of bioethanol (production of alcohol from the participating cellulose), and production hydrolysate milk (devoid of milk lactose)

Measurement of B-d mixing using opposite-side flavor tagging

We report on a measurement of the B-d(0) mixing frequency and the calibration of an opposite-side flavor tagger in the D0 experiment. Various properties associated with the b quark on the opposite side of the reconstructed B meson are combined using a likelihood-ratio method into a single variable with enhanced tagging power. Its performance is tested with data, using a large sample of reconstructed semileptonic B ->mu(DX)-X-0 and B ->mu(DX)-X-* decays, corresponding to an integrated luminosity of approximately 1 fb(-1). The events are divided into groups depending on the value of the combined tagging variable, and an independent analysis is performed in each group. Combining the results of these analyses, the overall effective tagging power is found to be epsilon D-2=(2.48 +/- 0.21(-0.06)(+0.08))%. The measured B-d(0) mixing frequency Delta m(d)=0.506 +/- 0.020(stat)+/- 0.016(syst) ps(-1) is in good agreement with the world average value.