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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    BJOG 86 (1979), S. 0 
    ISSN: 1471-0528
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background Organic acid anhydrides (OAAs) are highly allergenic compounds used in the chemical industry. The OAAs probably act as haptens but the proteins that form conjugates with OAAs in vivo are still unknown. Conjugates between the anhydrides and serum albumins (SAs) have routinely been used when testing for OAA-specific antibodies. However, the use of SA as the carrier-protein in these tests has never been evaluated.Objective The aim of this study was to identify major and also immunologically relevant protein conjugates of a particularly sensitizing OAA, hexahydrophthalic anhydride (HHPA), in plasma.Methods Plasma was obtained from a HHPA-exposed worker, from a guinea-pig (GP) exposed to HHPA in an exposure chamber for 2 weeks (8 h/day, 5 days/week) and from a GP exposed once, nose-only, to tritium-labelled HHPA for 8 h. The plasma was fractionated using ion exchange chromatography and gel filtration. These fractions and also aliquots of unfractioned plasma were hydrolysed, derivatized and analysed for anhydride adduct content using gas chromatography–mass spectrometry. Further, plasma from the tritium labelled HHPA-exposed GP was separated by SDS gel electrophoresis and analysed by autoradiography. In addition, immunologically relevant proteins were identified through specific IgE and IgG immunoblottings using sera from exposed workers.Results For humans 〉 85% and for GPs 〉 74% of the HHPA-adducts coeluted with SA in plasma. Autoradiography of GP-plasma shows a single 66 kDa protein that binds HHPA. IgE immunoblotting shows a major 66 kDa and a minor 28 kDa protein which could be inhibited by HHPA-SA conjugate. IgG immunoblotting showed a major 66 kDa protein and several minor protein bands.Conclusion This study shows SA to be the major protein in plasma that forms adducts in vivo with HHPA. The results also show that in an in vitro synthesized HHPA plasma protein conjugate, HHPA-specific IgE and IgG antibodies bind preferably to the SA.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 901 (1987), S. 255-264 
    ISSN: 0005-2736
    Keywords: (Human protein) ; Liposome ; Retinol transfer ; Retinol-binding protein ; Unilamellar liposome
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 944 (1988), S. 249-255 
    ISSN: 0005-2736
    Keywords: Phospholipid bilayer ; Retinol transport
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/General Subjects 714 (1982), S. 536-542 
    ISSN: 0304-4165
    Keywords: (Human liver) ; Retinol ; Retinol-binding protein
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 40 (1994), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: An Icelandic family with two cases of benign monoclonal gammopathy and one case each of Waldenström's macroglobulinaemia, histiocytic lymphoma and multiple myeloma was first described in 1978. Nine family members had then shown raised values for se-IgM. Of these one has since died and another was not available for testing. In four of the remaining seven se-IgM had returned to normal; the three subjects who still showed raised se-IgM included the case of multiple myeloma diagnosed in 1985. Baseline production of IgM, IgG and Ig in vitro was normal in the 35 family members studied compared with 13 healthy control subjects, but the mean production of all immunoglobulin classes in response to minimal stimulation with PWM (1 μg/ml) was significantly increased (P 〈0.05). Ten family members showed markedly increased production of all three immunoglobulin classes (〉 3 × SD above mean for controls). Raised production of IgM never occurred alone, indicating intact class switching. One family member showed extremely high values: IgA: 5.15 μg/ml, IgG: 16.3 μg/ml, IgM: 24.8 μg/ml (means for controls: 0.066, 0.123, 0.185 respectively). These 10 family members were of both sexes, ranged in age from 16 to 84 years and were clustered mainly in three distinct groups within the pedigree suggesting heredity. Proliferative responses to PWM were not significantly increased. Serum levels of interleukin-4 were tested in the patient with multiple myeloma and the family member with highest Ig production and found to be normal. We found no evidence for depressed NK function. Thus, in this family with a tendency for macroglobulinaemia and B cell derived malignancies B cell hyperreactivity was detectable by in vitro testing in several asymptomatic family members, of both sexes and a11 ages. No evidence was obtained for defects in regulatory mechanisms.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1573-4889
    Keywords: Ni-20Cr alloy ; corrosion ; water vapor ; whiskers ; TEM
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract Whiskers formed on the surface of a Ni-20Cr alloy during oxidation at high temperatures (1000 and 1200°C) were studied by scanning electron microscopy. The growth of these whiskers was attributed to the presence of water vapor in the atmosphere. The nature of these whiskers and their growth direction have been determined by electron diffraction with a transmission electron microscope (TEM). Their composition, determined by X-ray energy dispersive analysis (EDX), was NiCr2O4. The growth direction was of the (011) type.
    Type of Medium: Electronic Resource
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