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  • 1
    Electronic Resource
    Electronic Resource
    Site-selective spectroscopy and crystal-field analysis for Nd3+ in strontium fluorovanadate (1995)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 77 (1995), S. 270-276 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: Site-selective spectroscopy reveals that Nd3+ ions occupy more than 40 different crystal-field environments in Sr5(VO4)3F. Preferential energy transfer to the site responsible for 1 μm lasing occurs but becomes less complete with increasing temperature. The 4I and 4F3/2 Stark levels of the lasing site have been determined and an analysis of the crystal field performed. From the crystal-field fitting parameters Bkq, a calculated energy-level spectrum is determined up to 17 500 cm−1 with a rms deviation from the available experimental levels of 6 cm−1. © 1995 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.359387
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  • 2
    Electronic Resource
    Electronic Resource
    Optical spectra and analysis of Er3+ in silicon with C, O, and N impurities (1997)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 82 (1997), S. 2580-2583 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: Photoluminescence (PL) spectra of Er3+ in an Er-doped silicon film were recorded at 2 and 77 K over the wavelength range from 1.52 to 1.68 μm, which includes optical transitions between the Er3+ 4I13/2 and 4I15/2 manifolds. These spectra were then analyzed to determine the nature of the electrostatic field at the site of the Er ion that governs the ion's optical behavior. The PL spectra were analyzed three different ways: by considering the Er3+ ions to be occupying sites of Td, C3, or D2d point group symmetry. Transition energies and magnetic dipole transition probabilities were calculated for each case by diagonalizing a Hamiltonian representing the free-ion and crystal-field interactions in a Russell–Saunders basis of states spanning the lowest 15 J multiplets of the 4f11 electronic configuration of Er3+. Crystal-field parameters were varied in each case to find the best agreement with the experiment. Our results showed that the site symmetry of the Er3+ ions most consistent with the data is D2d. For this case, the rms deviation between the experimental and calculated energy levels is 3.3 cm−1 with the calculated magnetic dipole transition probabilities in qualitative agreement with the experiment. © 1997 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.366069
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  • 3
    Electronic Resource
    Electronic Resource
    Ribosomal proteins. 76. Protein-ribonucleic acid interactions in Escherichia coli ribosomes. Solution studies on S4-16S ribonucleic acid and L24-23S ribonucleic acid binding (1974)
    s.l. : American Chemical Society
    Biochemistry 13 (1974), S. 1032-1037 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00702a031
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  • 4
    Electronic Resource
    Electronic Resource
    Femoral venous flow dynamics during intraperitoneal and preperitoneal laparoscopic insufflation (1998)
    Springer
    Surgical endoscopy and other interventional techniques 12 (1998), S. 1213-1216 
    Details
    ISSN: 1432-2218
    Keywords: Key words: Laparoscopy — Inguinal hernia repair — Deep vein thrombosis — Femoral vein — Preperitoneal
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Background: Laparoscopic herniorrhaphy may be performed using an intraperitoneal or a preperitoneal approach. Anecdotal and experimental evidence indicates that alterations in lower extremity venous flow, which occur during intraperitoneal laparoscopic insufflation, may be associated with an increased risk of deep vein thrombosis. However, no study has directly compared femoral venous flow during intraperitoneal insufflation with that during preperitoneal insufflation. Method: In eight consecutive patients undergoing laparoscopic herniorrhaphy under general anesthesia, flow through the common femoral vein was evaluated with B-mode and color flow duplex. Pre- and intraperitoneal pressures were standardized to 10 mm Hg, and respiratory tidal volumes were standardized to 10 cc/kg. Flow measurements were taken at end expiration. Flow through the common femoral vein was measured after induction of anesthesia, during intraperitoneal insufflation, during preperitoneal insufflation, and between insufflations to ensure return to baseline. Results: All patients in the study were males. Their mean age was 59 years. Mean flow in the common femoral vein was essentially identical at baseline (138 ml/min) and during preperitoneal insufflation (135 ml/min). Alternatively, mean flow in the common femoral vein was significantly reduced during intraperitoneal insufflation (65 ml/min, p= 0.02). Conclusions: Flow in the common femoral vein is significantly reduced during intraperitoneal insufflation. However, flow in the common femoral vein is not affected by preperitoneal insufflation. These data suggest that laparoscopic preperitoneal inguinal hernia repair may pose as less a risk of thromboembolic complications than laparoscopic intraperitoneal inguinal hernia repair.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004649900823
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  • 5
    Electronic Resource
    Electronic Resource
    The accessibility of proteins of the Escherichia coli 30S ribosomal subunit to antibody binding (1973)
    Springer
    Molecular genetics and genomics 127 (1973), S. 89-110 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The accessibility of each of the proteins on the E. coli 30S ribosomal subunit was established by investigating whether or not immunoglobulins (IgG's) and their monovalent papain fragments (Fab's), specific for each of the 21 single ribosomal proteins, bind to the 30S subunit. The interpretation of the results of five different experimental approaches, namely Ouchterlony double diffusion and immunological “sandwich” methods, sucrose gradient and analytical ultracentrifugation, and functional inhibition tests, indicate that all 21 proteins of the 30S subunit have determinants available for antibody binding. There were quantitative differences between the degree of accessibility of the different ribosomal proteins. An attempt was made to correlate the results with the protein stoichiometric data of the small subunit proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00333659
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  • 6
    Electronic Resource
    Electronic Resource
    Accessibility of proteins in 50S ribosomal subunits of Escherichia coli to antibodies: An ultracentrifugation study (1977)
    Springer
    Molecular genetics and genomics 151 (1977), S. 245-252 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The accessibility of each of the proteins on the 50S ribosomal subunit of Escherichia coli was investigated by establishing whether immunoglobulins (IgG), specific for each of the 34 proteins from the 50S subunit, were able to bind to the 50S subunit. The main criterion for accessibility was the formation of specific antibody-50S subunit complexes that could be detected by means of analytical ultracentrifugation. The proteins fell into two main groups. Immunoglobulins against proteins L1, L2, L3, L4, L5, L6, L7/L12, L8, L9, L10, L11, L14, L15, L16, L17, L18, L19, L20, L21, L22, L23, L25, L26, L27 and L30 gave large amounts of complex (20–100%) and, therefore, these proteins were considered to be accessible sible on the surface of the 50S ribosomal subunit. The antibodies against the remaining proteins L13, L24, L28, L29 and L31 to L34 produced small amounts of complexes (10–20%). Since their effects were unequivocably stronger than those obtained with IgG's from sera of non-immunized animals, the results indicate that these proteins are probably also accessible. Nonetheless, from the ultracentrifugation studies alone definite conclusions about the exposure of the latter group of proteins could not be drawn.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00268787
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  • 7
    Electronic Resource
    Electronic Resource
    Proteins occurring at, or near, the subunit interface of E. coli ribosomes (1973)
    Springer
    Molecular genetics and genomics 127 (1973), S. 359-368 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The identification of ribosomal proteins that occur at, or near, the subunit interface of the 30S and 50S subunits in the E. coli 70S ribosome was attempted by studying the effect of antibodies on the Mg++ dependent dissociation-association equilibrium of 70S ribosomes. Dissociated ribosomes were mixed with monovalent fragments of IgG antibodies (Fab's) specific for each ribosomal protein and then reassociated into intact 70S particles. Various degrees of inhibition of this reassociation were observed for proteins S9, S11, S12, S14, S20, L1, L6, L14, L15, L19, L20, L23, L26 and L27. A small amount of aggregation of 50S subunits was caused by IgG's specific for the proteins S9, S11, S12, S14 and S20 and purified 50S subunits. It was inferred that the presence of small amounts of these proteins on 50S subunits was compatible with their presence at the subunit interface. Finally, the capacity of proteins S11 and S12 to bind to 23S RNA was demonstrated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00267106
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