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  • 1
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 97 (1992), S. 832-840 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: The b-type vibration–rotation band of N2⋅SO2 near the SO2 ν3 band origin was observed in a molecular-beam, diode laser direct absorption experiment. Rotational transitions and Stark effect data for this complex were additionally measured using molecular-beam electric resonance methods. The vibrational band origin was 1361.1440(2) cm−1, shifted by 0.9167(2) cm−1 from that of the SO2 monomer. Rotational constants were measured for the upper and lower vibrational states with A‘=8875.3(22) MHz, B‘=1620.3(22) MHz, C‘=1426.1(24) MHz, A'=8832.4(26) MHz, B'=1617.3(28) MHz, and C'=1431.6(15) MHz. The electric dipole moment components were determined, with μa = 0.0441(16) D and μc = 1.5884(29) D. The c component of the nitrogen quadrupole coupling component was found to be eqccQ = 1.30(21) MHz. A structure analysis gave the separation between the centers of mass of the monomers as 3.8925(28) A(ring). The angles between the symmetry axes of the SO2 and N2 units and the line connecting these monomers were calculated as 61.35° and 24.54°, respectively. Additionally, the SO2 monomer a axis was found to lie along the b axis of the complex. The electric dipole moment data indicate that the equilibrium angle for the SO2 is much closer to 90° than the rms result. These structural results were compared to model calculations of the binding energy of the complex.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science Ltd
    Clinical & experimental allergy 35 (2005), S. 0 
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background Hyper-responsiveness of nasal secretory function and volume changes are features of allergic rhinitis (AR) that are mediated in part by neural mechanisms. The finding of nasal hyper-responsiveness in subjects with AR who are currently symptomatic, but not in those who are currently out of season and asymptomatic, suggests that induction of neural reflexes in allergic subjects occurs as a result of allergic inflammation.Objectives To investigate whether allergen exposure in subjects with asymptomatic seasonal allergic rhinitis (SAR) may lead to induction of neural reflexes, and to investigate the components of the reflexes involved in this induction.Methods Asymptomatic subjects with (out-of-season) SAR underwent a nasal bradykinin challenge, before and 24 h after preceding ipsilateral (n=11) and contralateral (n=11) antigen challenge. Challenges were performed and nasal secretions collected using filter paper disks, and changes in nasal minimal cross-sectional area (Amin) were measured using acoustic rhinometry.Results Preceding ipsilateral antigen challenge led to the induction of a contralateral secretory reflex (P=0.01), which was absent in control experiments (P=0.34). Ipsilateral secretion weights were also enhanced. Preceding contralateral antigen challenge also induced a contralateral secretory reflex (P=0.03). Enhancement of the reduction in contralateral Amin was also seen (P=0.02). Ipsilateral responses were unchanged.Conclusions Allergen exposure in asymptomatic allergic subjects leads to induction of neural reflexes, resulting in nasal hyper-responsiveness, which persists beyond the resolution of the acute allergic response. Our data suggest that the mechanisms of allergen-induced hyper-responsiveness involve both afferent and efferent components.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 53 (1997), S. 461-463 
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Electron-transferring flavoprotein from the rumen bacterium Megasphaera elsdenii is a heterodimer (Mr = 75 kDa) containing FAD as cofactor and functioning solely to mediate electron transfer between the prosthetic groups of other proteins. The enzyme was crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol 4000 as precipitant. The crystals obtained belong to the space group P212121 with unit-cell dimensions of a = 58.75, b = 61.77 and c = 122.27 Å. Interestingly the crystals exhibit a low solvent content. Crystals diffracted to beyond 2.5 Å using synchrotron radiation.
    Type of Medium: Electronic Resource
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