MITOM: a new unfolding code based on a spectra model method applied to neutron spectrometry

The MITOM code was developed at UAB (Universitat Autònoma de Barcelona) for unfolding neutron spectrometric measurements with a Bonner spheres system (BSS). One of the main characteristics of this code is that an initial parameterisation of the neutron energy components (thermal, intermediate and fast) is needed. This code uses the Monte Carlo method and the Bayesian theorem to obtain a set of solutions achieving different criteria and conditions between calculated and measured count rates. The final solution is an average of the acceptable solutions. The MITOM code was tested for ISO sources and a good agreement was observed between the reference values and the unfolded ones for global magnitudes. The code was applied recently to characterise both thermal SIGMA and CANEL/T400 sources of the IRSN facilities. The results of these applications were very satisfactory as well.     

Prediction of work piece geometry in electrochemical cavity sinking

A computer-implemented model for predicting ECM work piece geometry has been developed and experimentally verified with a commercial ECM machine for cavity sinking in copper and 302-stainless steel with 2N K NO₃ electrolyte. Constant tool piece feed rates of 7–10 × 10^?4 cm/s, and applied voltages of 11–25 V were used. The model predicts the dependence of work piece geometry on operating conditions and on the electrochemical and physical properties of the metal—electrolyte pair. Comparison of eight equilibrium and six unsteady state experimental cavity profiles in copper showed satisfactory agreement with predictions, as did five equilibrium profiles for cavity sinking in 302-stainless steel.     

Velocity of surface carriers in inversion layers on silicon

Velocity-field curves for surface free-carriers in silicon are determined from measurements on resistivegate IGFETs. The measurements were performed on n-channel devices fabricated on both (100) and (111) substrates and on p-channel devices fabricated on (100) substrates. The channel length of the devices is ～8 μm and the impurity concentration of the substrates is ～ 10¹⁵ cm^?3. The dependence of velocity on the field strength along the channel is found to be well approximated by an empirical relationship involving three parameters: low-field mobility μ₀, a critical field $\text{E}{}_{\mathrm{cy}}$ signalling the onset of velocity saturation, and a parameter α that determines the curvature between the constant-mobility and constant-velocity branches of the curve. The curve-fitting parameters are given in tabular form for the two n-channel and one p-channel systems studied. The dependence of the velocity-field curves on temperatures in the range 100–350K is also reported.     

The effects of zinc and copper salts on Cyprinus carpio and Ctenopharyngodon idellus

The effects of zinc and copper salts on the survival of the two species of freshwater fish, common carp, Cyprinus carpio, and grass carp, Ctenopharyngodon idellus, were investigated. It was discovered that the levels of tolerance to the concentration of the metals were species-specific. Cyprinus carpio was found to be more susceptible to copper, whereas Ctenopharyngodon idellus was more susceptible to zinc. In general, copper was more toxic than zinc, as revealed by the survival times. The body and the gills of dead fish seemed to be covered by a veil-like film which looked like coagulated mucus and which was formed by the heavy-metal ions reacting with some constituents of the mucus and which was formed by the heavy-metal ions reacting with some constituents of the mucus secreted by the gill. The histopathological assessment of the gill and liver of Cyprinus carpio was also carried out. Particles were observed around the gills of the dead fish treated with zinc and copper salts, although no other major changes were found in the gill. Several histopathological changes were observed in the livers, including the presence of particles. The symptoms of the liver suggested that the internal injury was also an important feature of the intoxicants.     

Pasture intake and substitution rate effects on nutrient digestion and nitrogen metabolism during continuous culture fermentation

A continuous culture system was used to investigate ruminal digestion in response to increased pasture intake and three different substitution rates (SR) in a 4 x 4 Latin square design. The treatments were 1) low pasture (55 g dry matter (DM)/d, 2) medium pasture (MP, 65 g DM/d), 3) high pasture (75 g DM/d), and 4) pasture (45 g DM/d) plus concentrate (PC, 30 g DM/d). Treatments were designed to produce a low (0.33), medium (0.67), and high (1.00) SR (g of pasture/g of concentrate) by contrasting the low, medium, and high pasture intake treatments with the pasture plus concentrate treatment, respectively. Pasture was fed at 0630, 1000, 1730, and 2100 h, and concentrate at 0600 and 1700 h. Digestibility of DM and neutral detergent fiber were not affected by the amount of pasture. As the amount of pasture increased, pH decreased linearly, and total volatile fatty acid and NH3-N concentrations, and nonammonia N and bacterial N flows increased linearly. Concentrate supplementation did not affect DM digestibility at high SR but increased DM digestibility at low SR. Concentrate supplementation reduced pH and NH3-N concentrations at the three SR. Concentrate supplementation reduced the ratio of rumen degradable N to rumen degradable organic matter; however, the mechanism depended on the SR. High SR, concentrate supplementation reduced rumen degradable N, which reduced NIH-N concentration without affecting bacterial N flow. At low SR, concentrate supplementation increased rumen degradable organic matter, which reduced NH3-N concentration and increased bacterial N flow. Based on these results, at low SR, concentrate supplementation may enhance animal performance because of higher total DM intake and synthesis of microbial protein.     

Supplemental carbohydrate sources for lactating dairy cows on pasture

Two experiments were conducted to evaluate steam-flaked corn and nonforage fiber sources as supplemental carbohydrates for lactating dairy cows on pasture. Cows were allotted to a new paddock of an orchardgrass (Dactylis glomerata L.) pasture twice daily in one group in both trials. In experiment 1, 28 Holstein cows, averaging 216 d in milk, were randomly assigned to either a cracked-corn (CC) or a steam-flaked (SFC) supplement in a split plot design. The supplement contained 66.7% of corn and a protein/mineral pellet. In experiment 2, 28 Holstein cows, averaging 182 d in milk, were randomly assigned to either a ground corn (GC) or a nonforage fiber (NFF)-based supplemented in a single reversal design. The GC supplement contained 85% ground corn plus protein, mineral, and vitamins. The NFF supplement contained 35% ground corn, 18% beet pulp, 18% soyhulls, 8% wheat middlings plus protein, mineral, and vitamins. In both experiments, cows were fed the grain supplement twice daily after each milking at 1 kg/4 kg milk. In experiment 1, milk production (24.3 kg/d) and composition did not differ between treatments; however, plasma and milk urea N were lower with the SFC supplement. In experiment 2, milk production (27.5 kg/d) was not affected by treatments, which may be related to the medium quality of pasture grazed. The GC supplement tended to reduce plasma and milk urea N and increased milk protein percentage (3.23 vs. 3.19%). Pasture dry matter intake, measured using Cr2O3, did not differ between treatments in either experiment 1 (15.1 kg/d) or experiment 2 (12.2 kg/d). Milk production did not differ when mid-late lactation cows on pasture were supplemented with SFC or NFF instead of dry corn.     

Investigation of the morphotropic region in the Sr-doped lead hafnate-titanate solid solution Pb0.94Sr0.06Hf1-TixO3

Sr-doped lead hafnate titanate (PHT) oxides were synthesized by solid-state reaction and carefully studied in order to identify the reaction mechanisms. The reaction sequences in the formation of Sr-doped PbHfO₃, Sr-doped PbTiO}_{3 and Sr-doped PbHf_{1 - x}Ti_xO₃ were investigated using X-ray powder diffraction and differential thermal analysis. The Sr-doped PbHfO₃ oxide is mainly elaborated from the reaction between PbO and HfO₂, while Sr-doped PbTiO₃ oxide is formed from the reaction between Pb₃O₄ and TiO₂. The Sr-doped PbHf_1-xTi_xO₃ oxide is obtained from a solid-state reaction between Sr-doped PbHfO₃ and Sr-doped PbTiO₃ solid solutions. For x close to 0.5, tetragonal and rhombohedral ferroelectric phases coexist in a region commonly called the morphotropic region which presents the best dielectric and electromechanical properties. By means of X-ray powder diffraction, the boundaries of the morphotropic region in the (Pb_0.94Sr_0.06)Hf_1-xTi_xO₃ system have been determined for x ranging between 0.42 and 0.58. Finally, electrical and piezoelectric characterizations have been performed on Sr-doped PHT ceramics crystallizing in the morphotropic region. The compositional dependence of the electromechanical coupling factor (k_P), piezoelectric coefficients (d_{33 and g₃₃) and relative permittivity (_r) has been studied. An optimum composition has been determined as x equal to 0.51. © 2001 Kluwer Academic Publishers     

Deuterium NMR study of the MP-2269: albumin interaction — a step forward to the dynamics of non-covalent binding

MP-2269, the Gd(III) complex of 4-pcntylbicyclo[2.2.2] octane-l-carboxyl-di-L-aspartyl-lysinc-derived-DTPA, is a small Gd-agent that binds non-covalently to scrum albumin in vivo to assume the enhanced relaxivities associated with macromolecular agents, (due in part to increased rotational correlation time, τ_R). To further explore the fundamental parameters that govern the dynamics of water proton relaxation enhancement by this prototypical albumin-binding agent, the rotational correlation time (τ_R) for the deuterated La(III) analog of MP-2269 has been independently measured in the presence and absence of 4% albumin using²H-NMR approaches. The diamagnetic La(III) analog of MP-2269 was deuterated at the α-position of the carbonyl groups.²H-NMR studies were conducted at 7.05T (46 MHz) and 310°K on a Bruker NMR spectrometer. Spectral deconvolution permitted calculation of transverse relaxation rates, 1/T₂, from the NMR linewidths and subsequently, τ_R. The results yielded a τ_R of the albumin bound complex of ∼ 8 ns. This value is intermediate between those earlier estimated by¹⁷O-NMR (∼ 1 ns) and¹H-NMRD (∼ 20–50 ns) and significantly shorter than that of albumin. The²H-NMR study results also indicate that the exchange between free and albumin-bound forms of the La(III) analog is slow (exchange lifetimes > 1 ms). This slow exchange does not affect the water residence lifetimes (τ_M 140-280 ns).     

Improving Escherichia coli alkaline phosphatase efficacy by additional mutations inside and outside the catalytic pocket

We describe a strategy that allowed us to confer on a bacterial (E. coli) alkaline phosphatase (AP) the high catalytic activity of the mammalian enzyme while maintaining its high thermostability. First, we identified mutations, at positions other than those occupied by essential catalytic residues, which inactivate the bacterial enzyme without destroying its overall conformation. We transferred concomitantly into the bacterial enzyme four residues of the mammalian enzyme, two being in the catalytic pocket and two being outside. Second, the gene encoding the inactive mutant was submitted to random mutagenesis. Enzyme activity was restored upon the single mutation D330N, at a position that is 12 A away from the center of the catalytic pocket. Third, this mutation was combined with other mutations previously reported to increase AP activity slightly in the presence of magnesium. As a result, at pH 10.0 the phosphatase activity of both mutants D330N/D153H and D330N/D153G was 17-fold higher than that of the wild-type AP. Strikingly, although the two individual mutations D153H and D153G destabilize the enzyme, the double mutant D330N/D153G remained highly stable (T(m)=87 degrees C). Moreover, when combining the phosphatase and transferase activities, the catalytic activity of the mutant D330N/D153G increased 40-fold (k(cat)=3200 s-1) relative to that of the wild-type enzyme (k(cat)=80 s-1). Due to the simultaneous increase in K(m), the resulting k(cat)/K(m) value was only increased by a factor of two. Therefore, a single mutation occurring outside a catalytic pocket can dramatically control not only the activity of an enzyme, but also its thermostability. Preliminary crystallographic data of a covalent D330N/D153G enzyme-phosphate complex show that the phosphate group has significantly moved away from the catalytic pocket, relative to its position in the structure of another mutant previously reported.