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  • 1
    Electronic Resource
    Electronic Resource
    Interaction between Human IgD and Ricinus Agglutinin (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 24 (1986), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The results show that monoclonal IgD reacts specifically with ricinus agglutinin (molecular weight 120.000) (RcA1). The reaction between IgD and RcA1 was inhibited by galactose and lactose but not by glucose, indicating that the interaction is mediated by galactose containing carbohydrate units located in or near the σ-hinge region. Affinity chromatography on RcA1-Sepharose 4B was successfully used lo isolate monoclonal IgD from the IgD myeloma plasma.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1986.tb02068.x
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  • 2
    Electronic Resource
    Electronic Resource
    Identification of Cell Surface Immunoglobulin Markers by Protein A-Containing Fluorescent Staphylococci (1974)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 3 (1974), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: We describe a simple method for detecting surface-associated IgG on some human lymphoid cell lines and on mouse lymphocytes. using fluorescent Staphylococcus aureus (strain Cowan 1). The adherence of the fluorescent bacteria to cell surface-located IgG is mediated by protein A (SpA) molecules on the bacterial cell wall. Inhibition of the adherence of bacteria by soluble SpA was used for quantitation of IgG on cell surface. The method has a good specificity and a high sensitivity and detects approximately 600 IgG molecules per cell.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1974.tb01272.x
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  • 3
    Electronic Resource
    Electronic Resource
    Cell Separation by Staphylococcal Protein A-Coated Erythrocytes (1975)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 4 (1975), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: A method for cell separation according to cell surface markers is described. Heat-aggregated human IgG or IgG antibodies, raised to surface markers of mouse lymphocytes–for example, Ig or theta antigen–are allowed to react with the lymphocytes. When these cells are incubated with sheep erythrocytes coated with protein A of Staphylococcus aureus, rosettes are formed. These rosettes can be separated from nonrosetted lymphocytes by density gradient centrifugation. The erythrocytes of the rosettes are disrupted by complement action or by osmotic shock, and the lymphocytes are recovered. Immunoglobulin-protein A complexes are shed off the cell surfaces by cultivation. In this way cells with, as well as those without, surface markers could be obtained with high purity (up to 80%) and with high viability.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1975.tb02652.x
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  • 4
    Electronic Resource
    Electronic Resource
    Catabolism of the Murine IgGl Molecule: Evidence that Both CH2-CH3 Domain Interfaces are Required for Persistence of IgGl in the Circulation of Mice (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 40 (1994), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Site-directed mutagenesis of a recombinant Fc-hinge fragment has previously been used to identify a region of the murine IgG 1 molecule that controls catabolism, and this site encompasses amino acid residues at the interface of the CH2 and CH3 domains. In the current study the nature of this ‘catabolic site’ has been further analysed using recombinant techniques. Fc-hinge, CH2-hinge, CH2 and CH3 fragments have been expressed in Escherichia coli, purified and analysed in pharmacokinetic studies in mice. The CH2-hinge has been analysed as both a monomer and dimer, and the dimer has a longer β phase half-life (61.6 h) than the monomer (29.1 h). This suggests that two catabolic sites per Fc fragment are required for serum persistence. The need for two functional sites per molecule has been confirmed by the analysis of a hybrid Fc-hinge fragment comprising a heterodimer of one Fc-hinge with the wild type (WT) IgGl sequence and a mutant Fc-hinge with a defective catabolic site (mutated at His310, Gln311, His433 and Asn434). This hybrid is cleared with a β phase half-life of 37.9 h and this is significantly shorter than that of the WT Fc-hinge fragment (82.9 h). In contrast to the CH2-hinge dimer, the CH3 domain is cleared rapidly (β phase half-life of 21.3 h) indicating that the region of this domain (His433 and Asn434) previously identified as being involved in the control of catabolism is not sufficient in the absence of the CH2 domain for the serum persistence of an IgG fragment. The data extend our earlier observations concerning a region of the murine IgGl molecule that is involved in the control of catabolism and have implications for the design of engineered antibodies for therapy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1994.tb03488.x
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  • 5
    Electronic Resource
    Electronic Resource
    The Disappearance of SpA-IgG Antibody Complex on ‘Armed’ Lymphoid and Macrophages Cells (1978)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 7 (1978), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The disappearance rate of rabbit IgG antibody complexed with protein A from Staphylococcus aureus (SpA) on ‘armed’ mouse and rabbit spleen lymphocytes, and on ‘armed’ mouse peritoneal macrophages, was investigated by rosette and antibody-dependent cellular cytotoxicity (ADCC) assays. The half time of disappearance of complex from the surface of lymphoid cells was found to be 36 min in both assays. Macrophages, ‘armed’ with IgG antibody complexed with SpA, bind the corresponding antigens and subsequently lyse the target cells by extracellular and/or intracellular mechanisms. ‘Armed’ macrophages have both ADCC and phagocytosis ability, although a short half-time of disappearance of complex was observed (8 min).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1978.tb00463.x
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  • 6
    Electronic Resource
    Electronic Resource
    Arming of Lymphoid Cells by IgG Antibodies Treated with Protein A from Staphylococcus aureus (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 5 (1976), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Mouse spleen lymphocytes treated with rabbit IgG anti-sheep erythrocytes (SRBC) complexed with protein A of Stapbylococcus aureus (SpA) form rosettes with SRBC. The attachment of SRBC to lymphocytes was due to the binding of the SpA-IgG antibody complex to the surface of the lymphocytes and was thus considered ‘arming’ of the cells. Normal mouse spleen cells ‘armed’ with SpA-rabbit IgG anti-chicken erythrocytes (CRBC) kill specifically 51Cr-labeled CRBC ‘in vitro’ in the absence of free antibodies. The killing by these ‘armed’ cells is an effect of the cell-bound SpA-IgG antibody complex. Both the SRBC rosette formation and the cell-mediated CRBC killing was dependent on the concentration of the SpA-IgG antibody complexes used for ‘arming’ the cell. A 100-fold increase in rosette formation or in killing of target cells was recorded for lymphocytes treated with SpA-IgG antibody complexes in comparison with cell treated with noncomplexed IgG antibodies. The specific binding of SpA-IgG antibody complexes to the Fc receptors of mouse spleen cells was demonstrated by inhibition studies. More than 60% inhibition of the rosette formation and in the killing of target cells was shown for cell treated With normal rabbit IgG or its Fc fragment before addition of the SpA-IgG antibody complex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1976.tb00262.x
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  • 7
    Electronic Resource
    Electronic Resource
    A Method for the Detection and Quantitation of Fc Receptor Sites on Cells (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 5 (1976), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: A new rosette technique for identification of Fc-receptor-bearing cells is based on the ability of sheep erythrocyte coated with protein A of Staphylococcus aureus (ES) to form rosettes with cell treated with monomeric IgG or aggregated IgG. The IgG is attached to lymphocytes through its Fc region and to a trypsin-resistant but pronase sensitive receptor (considered an Fc receptor) The ES rosette technique facilitates studies of the interaction of IgG with Fc receptor sites; the binding of any IgG preparation reacting with protein A of Staphylococcus aureus (SpA) can be studied by the technique. Inhibition of rosette formation by SpA was used for quantitation of IgG fixed to the cell surface (that is, the number of Fc reception/cell). The sensitivity of the method permits quantitation of less than 105 IgG molecules bound to the Fc receptors. The relative affinity constant between Fc receptors and IgG ligands was estimated by plotting the percentage of ES rosettes as a function of IgG concentration and calculating the reciprocal of the IgG concentration giving half the maximal number of ES rosettes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1976.tb00263.x
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  • 8
    Electronic Resource
    Electronic Resource
    A selective model of plasma protein catabolism
    Amsterdam : Elsevier
    Journal of Theoretical Biology 90 (1981), S. 101-110 
    Details
    ISSN: 0022-5193
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0022-5193(81)90124-7
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  • 9
    Electronic Resource
    Electronic Resource
    An immunological hypothesis for plasma protein catabolism
    Amsterdam : Elsevier
    Mechanisms of Ageing and Development 17 (1981), S. 27-39 
    Details
    ISSN: 0047-6374
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0047-6374(81)90126-3
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  • 10
    Electronic Resource
    Electronic Resource
    A probabilistic approach to ageing and elimination of senescent plasma protein
    Amsterdam : Elsevier
    Mechanisms of Ageing and Development 23 (1983), S. 297-305 
    Details
    ISSN: 0047-6374
    Keywords: Ageing ; Catabolism ; Elimination ; Plasma proteins ; Probabilistic
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0047-6374(83)90030-1
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