Search Results - (Author, Cooperation:T. Do)

2012-10-09

American Association for the Advancement of Science (AAAS)

0036-8075

1095-9203

Biology

Chemistry and Pharmacology

Computer Science

Medicine

Natural Sciences in General

Physics

2011-11-05

Nature Publishing Group (NPG)

0028-0836

1476-4687

Biology

Chemistry and Pharmacology

Medicine

Natural Sciences in General

Physics

Animals ; Iris/anatomy & histology/cytology/*metabolism/*radiation effects ; Light Signal Transduction/physiology/*radiation effects ; Mammals/*physiology ; Mice ; Phospholipase C beta/metabolism ; Photic Stimulation ; Primates/physiology ; Reflex, Pupillary/physiology/radiation effects ; Retina/cytology/*metabolism/*radiation effects ; Retinal Ganglion Cells/metabolism/radiation effects ; Rod Opsins/*metabolism

1089-7690

AIP Digital Archive

Physics

Chemistry and Pharmacology

We report elastic and rotationally inelastic cross sections for e−–XH3 collisions (X: N, P, As, Sb) at the static-exchange level of approximation. The energy range was from 7.5 up to 30 eV. Our fixed-nuclei scattering amplitudes were obtained through the Schwinger multichannel method with pseudopotentials (SMCPP) [M. H. F. Bettega, L. G. Ferreira, and M. A. P. Lima, Phys. Rev. A 47, 1111 (1993)]. The rotational cross sections were obtained with the help of the adiabatic-nuclei-rotation approximation. There is good agreement with available experimental elastic cross sections. In order to improve rotational cross sections at small scattering angles for the dipole-allowed 00→10 rotational excitation, we have combined the SMCPP and the first Born approximation of the full interaction potential and also of the dipole moment potential. To our knowledge this is the first time that rotational excitation cross sections for these molecules are reported. © 1999 American Institute of Physics.

Electronic Resource

1089-7690

AIP Digital Archive

Physics

Chemistry and Pharmacology

We report elastic differential, integral, and momentum transfer cross-sections for H2X molecules (X: O, S, Se, and Te) obtained at the static exchange level of approximation. The energy range considered was from 2 up to 30 eV for H2O and from 5 up to 30 eV for the other molecules. Our calculations were performed with the Schwinger multichannel method with pseudopotentials [M. H. F. Bettega, L. G. Ferreira, and M. A. P. Lima, Phys. Rev. A 47, 1111 (1993)], combined with a Born closure procedure in order to account for the long-range potential due to the permanent dipole moment of the targets. Our calculated cross-sections for H2O and H2S are in good agreement with other theoretical results. Agreement with available experimental data is also encouraging. It was found that molecular size plays a crucial role in the scattering process. The influence of heavy and H atoms in the collisions is also discussed. For the integral cross-sections of the heavier molecules we also investigated incident energies below 5 eV, looking for possible shape resonances. Through the symmetry decomposition of the integral cross-sections and the eigenphase sum analysis, we found shape resonances for H2S, H2Se, and H2Te at the B2 symmetry. For H2Te, we have also found a shape resonance at the A2 symmetry. For all molecules a very broad structure was found at the A1 symmetry. This is the first work to report such resonances for H2Se and H2Te. © 1999 American Institute of Physics.

Electronic Resource

1077-3118

AIP Digital Archive

Physics

We have investigated the transport properties of a field-effect transistor (FET) with a composite quantum well, which consists of two adjacent semiconductor quantum wells, GaSb and InAs, sandwiched by AlSb barriers. This FET shows a novel V-shaped transfer characteristic, which is a direct result of the switching between electron and hole channels.

Electronic Resource

1365-3083

Blackwell Publishing Journal Backfiles 1879-2005

Medicine

αs1-Casein (CAS1_BOVIN), the major allergen of cow's milk (CM), is widely used as hydrolysates in infant diet formulae and additive to other processed food items. To date, most of the reported B-cell epitope mapping were performed on polyethylene pins or cellulose-derivative membrane. We sought to locate the motifs critical for human-specific IgE and rabbit polyclonal IgG binding using extensively purified CAS1_BOVIN, synthetic peptides and derivatives. Thirteen overlapping peptides covering the whole CAS1_BOVIN encompassing 17 : 20 amino acid (AA) were synthesized by f-moc AA solid-phase polyamide peptide synthesis. In addition, six cyanogen bromide (CNBr) cleavage fragments were prepared. Limited hydrolysis, oxidized and reduced/alkylated derivatives were also produced. The preparations were purified by ion exchange, gel filtration chromatography, reversed phase and high-performance liquid chromatography. The homogeneity was visualized by sodium dodecyl sulfate (SDS) and poly acryl amide gel electrophoresis (PAGE) followed by IgE and IgG immunoblotting. IgE binding was measured by Biotin Streptavidin (Bio/strep) fluoro enzyme immuno assay (FEIA) or ELISA-inhibition. Eighteen CM allergy (CMA) sera from 45 clinically examined children (Melbourne) and five adults (Bergen) were selected. Individual sera and pools were used for mapping IgE-binding epitopes. Rabbit IgG sera and pools were used for locating the antigenic sites of the molecule. Results indicated that all the individual CMA sera and pools recognized the intact molecule and three of the CNBr fragments as major antibody-binding allergens. The N- and C-terminal peptides (CAS 16-35; CAS 136-155) showed high IgE-binding affinity. CAS 1-18 and CAS 181-199 showed high IgG bindings. Considering the diversity of the antibody specificities, a reasonable agreement between IgE and IgG epitopes were found at the N- and C-terminals of CAS1_BOVIN. Mapping IgE B-cell epitopes by direct Bio/strep FEIA allowed the development of a sensitive modified technique for detecting unlabelled, casein immune dominant peptides in food products.

Electronic Resource

1365-3083

Blackwell Publishing Journal Backfiles 1879-2005

Medicine

Allergy to fish is common in Northern Europe. Variable reactions to different fish species are usually experienced among fish allergic patients. The allergens of cod fish and particularly the major allergen parvalbumin β (Gadus callarias) have been extensively studied in Norway. In the present communication, the white muscle parvalbumin was similarly found to be a major allergen in Atlantic salmon (Salmo salar, Sal s1 ). A purified salmon parvalbumin was obtained by anion exchange chromatography, gel filtration chromatography (GFC) and high-performance liquid chromatography (HPLC) of the muscle extracts. The antigenicity and allergenicity of salmon parvalbumin were confirmed using various immunologic and electrophoretic techniques. The protein is representative for several isoallergens judged by the amino acid (AA) sequence variance at certain sites in the AA sequence of CNBr cleavage peptides. Using sera from patients with cod and salmon allergy Sal s1 was demonstrated to be the major allergen of Atlantic salmon, as judged by RAST- and ELISA-inhibitions and crossed radioimmunoelectrophoresis (CRIE) techniques. The protein was also demonstrated to be antigenic by the use of polyclonal cod and salmon antibodies in IgG ELISA and immunoelectrophoretic methods. Cloning of parvalbumin cDNA from Atlantic salmon was performed based on an alignment of parvalbumin AA sequences from other species. A probe was generated by PCR and used for screening a salmon muscle cDNA-library. Subcloning and sequencing of two hybridizing clones revealed transcripts from two different parvalbumin genes. The translated sequences of both clones belong to the β-lineage of parvalbumins and include the entire coding region.

Electronic Resource

0039-6028

Elsevier Journal Backfiles on ScienceDirect 1907 - 2002

Physics

Electronic Resource

1435-604X

Keywords: Endothelial cell; Fluorescence detection; Laser microirradiation; Lutetium texaphryin; Photodynamic therapy; Photofrin II; Photosensitiser; Subcellular phototoxicity

Springer Online Journal Archives 1860-2000

Medicine

Physics

Technology

Abstract . Three cell types including bovine pulmonary artery endothelium cells (CPAE), rat kangaroo kidney cells (PTK2), and human larynx epidermoid carcinoma cells (Hep-2) were used to study subcellular localisation and phototoxicity of Photofrin-II and lutetium texaphyrin (Lu Tex). Cells were examined for fluorescence after administration of the photosensitisers. Subcellular regions were exposed with a laser microbeam system that used an argon ion laser pumped dye laser generating a 630 nm for Photofrin-II and 730 nm for Lu Tex. Fluorescence detection suggests that the Photofrin-II is bound primarily to the mitochondria with some diffuse fluorescence in the rest of the cytoplasm. The fluorescence in Lu Tex treated cells appears to be localised to the lysosomes. The percentage of damaged cells following light exposure to the different subcellular regions after Photofrin-II or Lu Tex treatment demonstrates that the nuclear region was the most sensitive target followed by the perinuclear region and peripheral cytoplasm region.

Electronic Resource