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  • 1975-1979  (4)
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Material
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Year
  • 1
    Electronic Resource
    Electronic Resource
    Kinetics of the Agglutination of IgG-coated Latex Particles by Clq: the Influence of Heat-labile Serum Components (1979)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 9 (1979), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Interaction between human Clq and IgG coaled latex particles has been studied by means of a standard aggregometer equipment. A dose-dependent agglutination was observed and 100 ng of Clq were readily detected. The kinetics of the agglutination was also monitored. Serum, partially puritied Cl, and high molecular weight fractions from Sephadex G-200 fractionated serum produced agglutination only in the presence of EDTA. In the absence of this chclator these products disintegrated prerormed Clq-IgG-latex particle agglutinates. This disagglutin-ating principle is heat-sensitive and tentatively macromolecular Cl dependent. The most probable basis of the activity is the competition between Cl, with a high affinity for IgG particles, and Clq. The inability of Cl to induce particle agglutination might be causetl by the Cl subunits Clr and Cls sterically inhibiting the subunit Clq to bridge between the panicles.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1979.tb03175.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Variations of Blood Eosinophils and Eosinophil Cationic Protein in Serum in Patients with Bronchial Asthma (1978)
    Oxford, UK : Blackwell Publishing Ltd
    Allergy 33 (1978), S. 0 
    Details
    ISSN: 1398-9995
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Inhalation challenge test was performed in 12 patients with bronchial asthma. The subsequent variation in blood eosinophils and serum-eosinophil canonic protein was followed up. Uniform patterns in both parameters were seen suggesting active participation of the eosinophil leucocyte in allergic: inflammation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1398-9995.1978.tb01536.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Cationic proteins of human granulocytes: Enhancement of phagocytosis ofStaphylococcus protein A-IgG complexes (1976)
    Springer
    Inflammation 1 (1976), S. 237-246 
    Details
    ISSN: 1573-2576
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The antibacterial chymotrypsin-like cationic protein of human granulocytes is shown to enhance the phagocytosis ofStaphylococcus protein A-IgG complexes by human granulocytes. The enhancement is time- and dose-dependent, and it is inhibited by heat inactivation of the chymotrypsin-like cationic protein. Granulocyte elastase and trypsin give a similar enhancement. The chymotrypsin-like cationic protein-mediated enhancement is poorly inhibited byα 1-antitrypsin. There is a need for approximately 20 molα 1-antitrypsin to inhibit 1 mol chymotrypsin-like cationic protein. Elastase is effectively inhibited at a 1∶1 molar relationship. Kinetic studies suggest that phagocytosis enhancement by chymotrypsin-like cationic protein may be due to modification of the Fc-receptor with concomitantly increased affinhy of the protein A-IgG complex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00917865
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Cationic proteins of human granulocytes Effects on human platelet aggregation and serotonin release (1976)
    Springer
    Inflammation 1 (1976), S. 359-370 
    Details
    ISSN: 1573-2576
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Immune-aggregate and thrombin-mediated [3H]serotonin release from human platelets are shown to be enhanced when platelets are preincubated with the antibacterial chymotrypsin-like cationic protein isolated from human granulocytes. The enhancement is dose dependent and inhibited by heating of the cationic protein. Release with chymotrypsin-like cationic protein alone was not observed, although the protein was shown to “micro-aggregate” platelets irreversibly by an ADP-dependent reaction. Platelet “macro-aggregation” induced by immune-aggregate was also enhanced by chymotrypsin-like cationic protein whereas platelet “macro-aggregation” induced by thrombin was inhibited competitively. Platelet “micro-aggregation” induced by chymotrypsin-like cationic protein was inhibited when preincubated for more than 5 min with a 2-fold molar excess ofα-1-antitrypsin. Chymotrypsin-like cationic protein interaction with several platelet reactions suggests a close relationship between neutrophils and platelets in the inflammatory process.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00920337
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    Paper (German National Licenses)
    Fulltext
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