998 resultados para FULL HYDRATION


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The effect of application methods and dentin hydration on the bond strength of three self-etching adhesives (SEA) were evaluated; 195 extracted bovine incisors were used. The buccal surface was ground in order to expose the dentin, which remained 2-mm minimum thickness, measured by a thickness meter through an opening on the lingual surface. Adper Single Bond 2 (TM) was used for the control group. The SEA were applied following two modes of application: passive or active and two hydration states of the dentin surface-dry and wet. After light-curing, composite buildups were made using Grandio (TM) composite. The specimens were sectioned and tested with a microtensile bond strength test. The application method and the hydration state resulted in statistical differences (p = 0.000) making the values of active application for mu TBS to dentin higher than passive application. The wet surfaces showed higher mu TBS to dentin ratios than dry surfaces. There were no statistical differences in mu TBS among the SEA tested but there were differences regarding to control group.

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Purpose: To evaluate the effect of surface hydration state and application method on the microtensile bond strength of one-step self-etching adhesives systems to cut enamel.Materials and Methods: One hundred ninety-five bovine teeth were used. The enamel on the buccal side was flattened with 600-grit SiC paper. For the control group, 15 teeth received Adper Single Bond 2, applied according to manufacturer's recommendations. The other specimens were divided into three groups according to the adhesive system used: Futura Bond M (FM; Voco), Clearfil S-3 Bond (CS; Kuraray), and Optibond All in One (OA; Kerr). For each group, two hydration states were tested: D: blown dry with air; W: the excess of water was removed with absorbent paper. Two application methods were tested: P (passive): the adhesive was simply left on the surface; A (active): the adhesive was rubbed with an applicator point. A coat of Grandio composite resin (Voco) was applied on the surface. The teeth were sectioned to obtain enamel-resin sticks (1 x 1 mm), which underwent microtensile bond testing. The data in MPa were submitted to a three-way ANOVA and Tukey's test (alpha = 5%).Results: The ANOVA showed significant differences for application method and the type of adhesive, but not for hydration state. For the application method, the results of Tukey's test were: P: 31.46 (+/-7.09)a; A: 34.04 (+/-7.19)b. For the type of adhesive, the results were: OA: 31.29 (+/-7.05)a; CS: 32.28 (+/-7.14)a; FM: 34.68 (+/-7.17)b; different lower-case letters indicate statistically significant differences.Conclusion: Active application improved the bond strength to cut enamel. The adhesive Futurabond M showed the highest bond strength to cut enamel.

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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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Direct and simultaneous measurements of hydration water content and protein conformation have been performed using quartz crystal microbalance and visible absorption spectroscopy. Equilibrium and kinetics of methaemoglobin/haemichrome transition induced by the alteration of the degree of hydration was investigated in thin films exposed to controlled humidity. The kinetics experiment show that the conversion of species achieve the equilibrium more rapidly that the amount of sorbed water by the protein. The transition shows a sigmoid behaviour and suggest cooperative phenomena manifested by haem-haem interaction. The water hydration network contributing to the haem haem interaction advise that water acts as allosteric effectors for the conversion between species. Irreversible changes produced by complete drying are clearly shown.

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The local environment of Er3+ ions in microporous titanosilicate ETS-10 and in synthetic narsarsukite and glassy materials obtained by calcination of ETS-10 has been investigated by EXAFS, Raman and photoluminescence spectroscopies. Er L-III-edge EXAFS studies of Er3+-doped ETS-10 support the view that the exchanged Er3+ ions reside close to the (negatively charged) TiO6 octahedra. In ETS-10, Er3+ is partially bonded to framework oxygen atoms and hydration water molecules. The Er...Ti distance (3.3 Angstrom) is similar to the Na...Ti distances (3.15-3.20 Angstrom) reported previously for Na-ETS-10. Although the exact location of the ErO6 units within the host structure of Er3+-doped synthetic narsarsukite is still an open question, it is most likely that Er3+ substitutes Ti4+ rather than Na+ ions. EXAFS spectroscopy indicates that no significant clustering of erbium atoms occurs in the titanosilicate samples studied. Evidence for the insertion of Er3+ ions in the framework of narsarsukite has been obtained by Raman spectroscopy. This is indicated by the increasing full-width at half-maximum (FWHM) of the 775 cm(-1) peak and the increasing intensity of the anatase peaks as the erbium content increases. In addition, as the narsarsukite Er3+ content increases a band at ca. 515 cm(-1) firstly broadens and subsequently a new peak appears at ca. 507 cm(-1).Er3+-doped narsarsukite exhibits a characteristic local vibrational frequency, (h) over bar omega ca. 330 cm(-1), with an electron-phonon coupling, g ca. 0.2, which constitutes additional evidence for framework Er3+ insertion. The number of lines in the infrared emission spectrum of synthetic narsarsukite indicates the presence of two optically-active erbium centres with very similar local environments and an average I-4(13/2) lifetime of 7.8 +/- 0.2 ms.

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The effect of anions on the stability of different functional conformations of Hb is examined through the determination of the dependence of O-2 affinity on water activity (a(w)). The control of a(w) is effected by varying the sucrose osmolal concentration in the bathing solution according to the osmotic stress method. Thus, the hydration change following Hb oxygenation is determined as a function of Cl- and of DPG concentration. We find that only similar to 25 additional water molecules bind to human Hb during the deoxy-to-oxy conformation transition in the absence of anions, in contrast with similar to 72 that bind in the presence of more than 50 mM Cl- or more than 15 mu M DPG. We demonstrate that the increase in the hydration change linked with oxygenation is coupled with anion binding to the deoxy-Hb. Hence, we propose that the deoxy-Hb coexists in two allosteric conformations which depend on whether anion is bound or not: the tense T-state, with low oxygen affinity and anion bound, or a new allosteric P-state, with intermediate oxygen affinity and free of bound anions. The intrinsic oxygen affinity of this unforeseen P-state and the differential binding of Cl-, DPG, and H2O between states P and T and P and R are characteristics which are consistent with those expected for a putative intermediate allosteric state of Hb. These findings represent a new opportunity to explore the structure-function relationships of hemoglobin regulation.

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We have measured hemoglobin oxygen uptake vs. The partial pressure of oxygen, with independently controlled activities of chloride and water. This control is effected by combining different concentrations of NaCl and sucrose in the bathing solution to achieve: (i) water activities were varied and CI- activity was fixed, (ii) both water and CI- activities were varied with a traditional NaCI titration, or (iii) CI- activities were varied and water activity was fixed by adding compensating sucrose. Within this analysis, the CI--regulated loading of four oxygens can be described by the reaction Hb.CI- + 4 O-2 + 65 H2O reversible arrow Hb.4O(2).65H(2)O + CI-. The dissociation of a neatly integral chloride, rather than the nonintegral 1.6 chlorides inferred earlier from simple salt titration, demonstrates the need to recognize the potentially large contribution from changes in water activity when titrating weakly binding solutes. The single-chloride result might simplify structural considerations of the action of CI- in hemoglobin regulation.