Localization of collisionally inhomogeneous condensates in a bichromatic optical lattice

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

Localization of a Bose-Fermi mixture in a bichromatic optical lattice

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

Matter-wave localization in a weakly perturbed optical lattice

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

Nucleotide sequence, genomic organization and chromosome localization of 5S rDNA in two species of Curimatidae (Teleostei, Characiformes)

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

Localization of the optimal solution and a posteriori bounds for aggregation

After an aggregated problem has been solved, it is often desirable to estimate the accuracy loss due to the fact that a simpler problem than the original one has been solved. One way of measuring this loss in accuracy is the difference in objective function values. To get the bounds for this difference, Zipkin (Operations Research 1980;28:406) has assumed, that a simple (knapsack-type) localization of an original optimal solution is known. Since then various extensions of Zipkin's bound have been proposed, but under the same assumption. A method to compute the bounds for variable aggregation for convex problems, based on general localization of the original solution is proposed. For some classes of the original problem it is shown how to construct the localization. Examples are given to illustrate the main constructions and a small numerical study is presented.

Immunocytochemical localization of heparin in secretory granules of rat peritoneal mast cells using a monoclonal anti-heparin antibody (ST-1)

We performed immunogold labeling with an ST-1 monoclonal antibody (IgM), specific for intact heparin, to define the subcellular localization of heparin in mast cells. Rat peritoneal mast cells were fixed by a modified Karnovsky method and embedded in Araldite. Ultrathin sections were first treated with sodium periodate and then sequentially incubated with MAb ST-1, rabbit anti-mouse IgM, and protein A-gold. By transmission electron microscopy, gold particles were localized inside cytoplasmic granules of peritoneal mast cells. In contrast, with the same procedure, no labeling was observed in mast cells from rat intestinal mucosa. Control sections of rat peritoneal or intestinal mucosa mast Mast cells cells treated with an irrelevant MAb (IgM) did not show any labeling. Treatment with nitrous Heparin acid abolished the reactivity of MAb ST-1 with peritoneal mast cells. These results Granules show that different mast cells can be identified regarding their heparin content by immunochemical procedures using MAb ST-1.

Energy localization in the Phi(4) oscillator chain

We study energy localization in a finite one-dimensional Phi(4) oscillator chain with initial energy in a single oscillator of the chain. We numerically calculate the effective number of degrees of freedom sharing the energy on the lattice as a function of time. We find that for energies smaller than a critical value, energy equipartition among the oscillators is reached in a relatively short time. on the other hand, above the critical energy, a decreasing number of particles sharing the energy is observed. We give an estimate of the effective number of degrees of freedom as a function of the energy. Our results suggest that localization is due to the appearance, above threshold, of a breather-like structure. Analytic arguments are given, based on the averaging theory and the analysis of a discrete nonlinear Schrodinger equation approximating the dynamics, to support and explain the numerical results.

Localization and irregular distribution of Na,K-ATPase in myelin sheath from rat sciatic nerve

Sodium, potassium adenosine triphosphatase (Na,K-ATPase) is a membrane-bound enzyme that maintains the Na+ and K+ gradients used in the nervous system for generation and transmission of bioelectricity. Recently, its activity has also been demonstrated during nerve regeneration. The present study was undertaken to investigate the ultrastructural localization and distribution of Na,K-ATPase in peripheral nerve fibers. Small blocks of the sciatic nerves of male Wistar rats weighing 250-300g were excised, divided into two groups, and incubated with and without substrate, the para-nitrophenyl phosphate (pNPP). The material was processed for transmission electron microscopy, and the ultra-thin sections were examined in a Philips CNI 100 (TM) electron microscope. The deposits of reaction product were localized mainly on the axolemma, on axoplasmic profiles, and irregularly dispersed on the myelin sheath, but not in the unmyelinated axons. In the axonal membrane, the precipitates were regularly distributed on the cytoplasmic side. These results together with published data warrant further studies for the diagnosis and treatment of neuropathies with compromised Na,K-ATPase activity. (c) 2007 Elsevier Ltd. All rights reserved.

Energy localization in the Peyrard-Bishop DNA model

We study energy localization on the oscillator chain proposed by Peyrard and Bishop to model DNA. We search numerically for conditions with initial energy in a small subgroup of consecutive oscillators of a finite chain and such that the oscillation amplitude is small outside this subgroup on a long time scale. We use a localization criterion based on the information entropy and verify numerically that such localized excitations exist when the nonlinear dynamics of the subgroup oscillates with a frequency inside the reactive band of the linear chain. We predict a mimium value for the Morse parameter (mu>2.25) (the only parameter of our normalized model), in agreement with the numerical calculations (an estimate for the biological value is mu=6.3). For supercritical masses, we use canonical perturbation theory to expand the frequencies of the subgroup and we calculate an energy threshold in agreement with the numerical calculations.

Electrophoretic variants of intracellular catalase of different Candida species

Intracellular and extracellular catalases of different species of Candida were investigated using different culture media. All the Candida strains produced intracellular catalase, whose enzymatic activity was detected by non-denaturating polyacrylamide gradient (4-30%) gel electrophoresis. The cell extracts presented a major 230 kDa catalase band and in some strains variants of catalase with different molecular weights were detected. Candida catalase activity was not affected by heating at 50degreesC and incubation with beta-mercaptoethanol, but treatment with sodium dodecyl sulphate inhibited or reduced enzymatic activity. Extracellular enzyme activity was not detected in any of the culture filtrate extracts tested.