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  • 1
    Electronic Resource
    Electronic Resource
    A new digital all-sky imager experiment for optical auroral studies in conjunction with the Scandinavian twin auroral radar experiment (1998)
    [S.l.] : American Institute of Physics (AIP)
    Review of Scientific Instruments 69 (1998), S. 578-584 
    Details
    ISSN: 1089-7623
    Source: AIP Digital Archive
    Topics: Physics , Electrical Engineering, Measurement and Control Technology
    Notes: Studies of the relationship between the optical aurorae and the ionospheric electric fields, as observed by the bi-static Scandinavian twin auroral coherent backscatter radar experiment (STARE) and the tri-static European incoherent backscatter radar facility (EISCAT), are to be undertaken in Scandinavia. For this purpose, an unmanned and fully automatic low-light-level television camera system, coupled to an all-sky lens, has been constructed. A personal computer controls all aspects of the instrument, operating it for all dark and moon-free periods. Monochrome optical data, usually at 557.7 nm, are pre-processed in real time at the recording site. The transformed images are stored digitally to magneto-optical disk with a temporal and spatial resolution directly compatible with the STARE radar data, thus making comparisons easy. Simultaneous TV recordings to tape may be made on a campaign basis. The camera has been calibrated for all gain settings, thereby permitting auroral images to be recalled in any sequence with the same absolute intensity scale. Modem communication permits remote control, trouble shooting and quick-look data transfers. © 1998 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.1148697
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  • 2
    Electronic Resource
    Electronic Resource
    Activation of the Complement, Coagulation, Fibrinolytic and Kallikrein–Kinin Systems During Attacks of Hereditary Angioedema (1996)
    Oxford, U.K. and Cambridge, USA : Blackwell Science Ltd
    Scandinavian journal of immunology 44 (1996), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Five patients with hereditary angioedema (HAE) were studied during attacks and remission as were healthy controls. The high levels of C1/C1-INH complexes, low C4 and high ratio C4 activation products (C4bc)/C4 also differed significantly during remission compared to controls.During attacks C4bc/C4 increased (922–2007; P=0.022, remission versus attacks, median values throughout), C2 and CH50 dropped (111–31%; P=0.043 and 110–36%; P=0.016, respectively), TCC (C5b-9) increased (0.88–1.23 AU/ml; P=0.028). Cleavage of HK increased to be almost complete during attacks (20–90%; P=0.009). While factor XIa/serpin-complexes did not increase, a more than twofold rise in thrombin/antithrombin-complexes (0.20–0.50 μg/l; P=0.009) and in plasmin/alpha-2-antiplasmin-complexes (7.3–17 nmol/l; P=0.028) was observed. For the first time cascade activation in HAE was studied simultaneously, and corroborates that attacks lead to activation of the kallikrein-kinin system, fibrinolysis and early part of the classical complement pathway. In addition, the authors present novel data of terminal complement and coagulation activation, the latter apparently not via FXIa.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-3083.1996.d01-298.x
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  • 3
    Electronic Resource
    Electronic Resource
    Isolation and Characterization of Porcine Mannan-Binding Proteins of Different Size and Ultrastructure (1996)
    Oxford, U.K. and Cambridge, USA : Blackwell Science Ltd
    Scandinavian journal of immunology 43 (1996), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The authors report on the purification and characterization of mannan-binding proteins (MBP) isolated from porcine serum. The MBPs were purified by use of PEG precipitation, affinity chromatography on mannan-Sepharose, protein A- and anti-porcine IgM-Sepharose followed by gel filtration. The MBP proteins were collagenase sensitive and showed γ1-γ2-electrophoretic mobility. The MBP designated pMBP-28 had a molecular mass of 28 kDa when analysed on SDS-PAGE under reducing conditions and eluted corresponding to a molecular mass of approximately 700 kDa on gel filtration chromatography. Electron micrographs of pMBP-28 revealed an oligomeric protein similar to rodent MBP-A and human MBP but with a predominance of penta- and hexameric molecules. Another protein designated pMBP-27 was composed of peptides of 27 kDa and had an Mr of 300–350 kDa on gel filtration chromatography. Electron microscopy of pMBP-27 showed dimer and trimer molecules; the trimers without distinct stalk regions. The N-terminal 26 (pMBP-27) and 24 (MBP-28) amino acid residues showed 54% and 58% identity with human MBP. pMBP-28 showed a higher degree of sequence similarity to rat and mouse MBP-A (60% identity) than to mouse and rat MBP-C (41–45% identity). Both pMBPs exhibited Ca2+-dependent binding to D-mannose immobilized on agarose but no significant binding to N-acetyl-D-glucosamine- or fucose-agarose. The results further suggested the presence of a third pMBP which copurified with pMBP-27 but this protein was not sequenced.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-3083.1996.d01-39.x
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  • 4
    Electronic Resource
    Electronic Resource
    A chilling-sensitive mutant of Arabidopsis is deficient in chloroplast protein accumulation at low temperature (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Plant, cell & environment 18 (1995), S. 0 
    Details
    ISSN: 1365-3040
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Mutations at the chsl locus in Arabidopsis thaliana (L.) confer a chilling-sensitive phenotype in which plants become chlorotic and die after more than 3 d of exposure to temperatures in the range of 18 to 10°C. Within 8h after transfer of mutant plants from growth at 23 to 13°C, accumulation of the newly synthesized chloroplast-localized polypeptides stearoyl-ACP desaturase, glutamine synthetase and OEC 23 was severely impaired. By contrast, there was no apparent deleterious effect on the accumulation of two extrachloroplastic proteins examined: the elongation factor lα, and the phloem-specific, extrachloroplastic isoform of glutamine synthetase. In one instance examined in detail, chilling did not decrease the accumulation of mRNA for stearoyl-ACP desaturase, indicating that the effect was post-transcriptional. Chloroplasts isolated from chilled wild-type and chsl plants were equally able to process and protect from protease digestion in vitro synthesized pre-plastocyanin. The results suggest that the chsl mutant may be defective in some aspect of chloroplast protein accumulation at low temperature.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3040.1995.tb00540.x
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  • 5
    Electronic Resource
    Electronic Resource
    Binding of Complement Proteins C1q and C4bp to Serum Amyloid P Component (SAP) in Solid Contra Liquid Phase (1996)
    Oxford, U.K. and Cambridge, USA : Blackwell Science Ltd
    Scandinavian journal of immunology 44 (1996), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Serum amyloid P component (SAP), a member of the conserved pentraxin family of plasma proteins, binds calcium dependently to its ligands. The authors investigated SAPs interaction with the complement proteins C4b binding protein (C4bp) and C1q by ELISA, immunoelectrophoresis and electron microscopy. Binding of these proteins to SAP was demonstrated when SAP was immobilized using F(ab′)2 anti-SAP, but not when SAP reacted with these proteins in liquid phase; thus the binding to human SAP was markedly phase state dependent. Presaturation of solid phase SAP with heparin, which binds SAP with high affinity, did not interfere with the subsequent binding of C4bp or C1q to SAP. In contrast, collagen I and IV showed partial competition with the binding of C1q to SAP. Using fresh serum, immobilized native SAP bound C4bp whereas binding of C1q/C1 could not be demonstrated. Altogether the results indicate that firm binding of C1q and C4bp to SAP requires that SAP is presented on a solid phase, that C1q and C4bp react with sites distinct from the heparin binding site, and that C1q and collagen I share binding sites on SAP. Immobilized native SAP, aggregated SAP and SAP-heparan-sulphate complexes induced no detectable complement activation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-3083.1996.d01-326.x
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  • 6
    Electronic Resource
    Electronic Resource
    A Neoepitope-Based Enzyme Immunoassay for Quantification of C1-Inhibitor in Complex with C1r and C1s (1997)
    Oxford, UK : Blackwell Science Ltd
    Scandinavian journal of immunology 46 (1997), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Monoclonal antibodies (MoAb) recognizing neoepitopes exposed on activation products of complement proteins but hidden in the native components have been used for quantification of activated complement. A previously produced and characterized mouse MoAb, recognizing a neoepitope on the human plasma protein C1-inhibitor complexed with its substrates, was used to design an enzyme immunoassay for detection of C1-inhibitor complexed with C1r and C1s. These complexes are indicators of early classical complement pathway activation. The standard was serum activated with heat aggregated IgG defined to contain 1000 arbitrary units (AU)/ml. The lower detection limit was ≈0.05 AU/ml corresponding to 0.005% of fully activated serum. The reliability of the assay, including day-to-day variation, was tested. Intra-assay variation coefficients were 12% for low plasma control and 13% for high plasma control (n = 12 for both). Inter-assay variation coefficients were 12% for low control (n = 6), 19% for high control (n = 6) and 15% for the normal plasma control (n = 9). A 2.5–97.5 percentile reference range (normal blood donors) was 16–33 AU/ml. Two patients with systemic lupus erythematosus had considerably elevated plasma levels of the activation product (56 and 62 AU/ml), and six patients with hereditary angioedema had normal plasma levels despite considerably reduced C1-inhibitor concentration. We conclude that the present method is sensitive and reliable for detection of early classical pathway activation and superior to previously published methods by utilizing neoepitope specificity and non-radiolabelled reagents.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-3083.1997.d01-168.x
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  • 7
    Electronic Resource
    Electronic Resource
    Serum Amyloid P Component Binds to Influenza A Virus Haemagglutinin and Inhibits the Virus Infection In Vitro (1997)
    Oxford, UK : Blackwell Science Ltd
    Scandinavian journal of immunology 46 (1997), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Serum amyloid P component (SAP) is a member of the phylogenetically conserved and structurally related group of proteins called pentraxins. SAP exhibits multispecific calcium-dependent binding to oligosaccharides with terminal N-acetyl-galactosamine, mannose and glucuronic acid. The authors report that SAP can bind to influenza A virus and inhibit agglutination of erythrocytes mediated by the virus subtypes H1N1, H2N2 and H3N2. SAP also inhibits the production of haemagglutinin (HA) and the cytopathogenic effect of influenza A virus in MDCK cells. The binding of SAP to the virus requires physiological calcium concentrations and is blocked by specific SAP antibodies. Denaturated and renaturated SAP retained inhibition of HA. Electron microscopy shows Ca2+-dependent binding of SAP to spikes on the viral envelope and immunoblotting indicates that SAP binds to a 50–55 kDa peptide corresponding to the mass of the HA1 peptide. Of several monosaccharides tested only D-mannose interfered with SAP's inhibition of both HA and infectivity. The glycosaminoglycans heparan sulfate and heparin, which bind SAP, reduced SAPs binding to the virus. The results indicate that the inhibition by SAP is due to steric effects when SAP binds to terminal mannose on oligosaccharides localized close to the sialic acid-binding site of the HA trimer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-3083.1997.d01-147.x
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  • 8
    Electronic Resource
    Electronic Resource
    C3 is Activated in Hereditary Angioedema, and C1/C1-Inhibitor Complexes Rise During Physical Stress in Untreated Patients (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 42 (1995), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Seven patients witb hereditary angioedema (HAE) were studied to understand further how physical exercise may induce attacks. The most pronounced differences between patients and controls, however, were independent of the controlled bicycle run (mean values in patients/controls); C4(g/L): 0.12/0.28 (P= 0.0122); C4bc (AU/ml): 137.0/18.0 (P = 0.0002); C4d (mg/mL): 5.03/2.35 (P = 0.0004); C3bc (AU/ml): 8.4/6.3 (P= 0.0049); C3a (AU/ml): 11.1/5.6 (P= 0.0102). The ratio C4bc to C4 was 1141 versus 64. Consequently, a substantial part of the low amount of C4 left in HAE patients consists of activation products, and the authors show for the first time that a mild but significant activation of C3 occurs in HAE. The two HAE patients treated with danazol had values of Cl-INH function and antigen, C4, and C2 in-between those of normal and untreated patients, and lower levels of split products from C4 and high molecular weight kininogen than untreated patients. As a result of the exercise, fibrinolysis increased significantly in both patients and controls, while C1/Cl-INH complexes rose significantly only in the five HAE patients without treatment when compared to the seven controls (P= 0.0089). This study thus suggests that complement activation is enhanced in untreated HAE patients following physical stress.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1995.tb03711.x
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  • 9
    Electronic Resource
    Electronic Resource
    Mannan-Binding Protein Forms Complexes with α-2-Macroglobulin. A Proposed Model for the Interaction (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 42 (1995), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: We report that α-2-macroglobulin (α2M) can form complexes with a high molecular weight porcine mannan-binding protein (pMBP-28). The α2M/pMBP-28 complexes were isolated by PEG-precipitation and affinity chromatography on mannan-Sepharose, protein A-Sepharose and anti-IgM Sepharose. The occurrence of α2M/pMBP-28 complexes was further indicated by crossed immunoelectrophoresis and by use of an anti-α2M affinity column and chelating Sepharose loaded with Zn2+. The eluates from these affinity columns showed α2M subunits (94 and 180 kDa) and pMBP subunits (28 kDa) in SDS-PAGE, which reacted with antibodies against α2M and pMBP-28, respectively, in Western blotting. Furthermore, the α2M/pMBP-28 complexes were demonstrated by electron microscopy, Fractionation of pMBP-containing D-mannose eluate from mannan-Sepharose on Superose 6 showed two protein peaks which reacted with anti-C1 s antibodies in ELISA, one of about 650–800 kDa, which in addition contained pMBP-28 and anti-α2M reactive material, the other with an Mr of 100–150 kDa. The latter peak revealed rhomboid molecules (7 × 15 nm) in the electron microscope and a 67 kDa band in SDS-PAGE under reducing conditions. This band was also seen in eluates from the anti-α2M and chelating Sepharose columns. Based on these observations and previous findings by other investigators of a serine protease with about 67 kDa subunits which copurifies with human MBP we propose a model for the interaction of pMBP-28 with α2M.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1995.tb03670.x
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  • 10
    Electronic Resource
    Electronic Resource
    Improved primer sequences for the mitochondrial ND1, ND3/4 and ND5/6 segments in salmonid fishes: application to RFLP analysis of Atlantic salmon (1998)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of fish biology 53 (1998), S. 0 
    Details
    ISSN: 1095-8649
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: New specific primers for the mtDNA segments ND1, ND3/4 and ND5/6 designed from the rainbow trout sequence, improved PCR amplification for salmonid fishes. RFLP analysis revealed restriction site variation for all three segments in Atlantic salmon. Eleven haplotypes were detected in a screening of 30 individuals from four European populations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1095-8649.1998.tb00122.x
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