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  • 1975-1979  (12)
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Year
  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 10 (1979), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: In this study we present evidence that SAA is complexed to high density lipoprotein (HDL) in rabbit serum and is co-isolated with HDL apoproteins. The binding of SAA to HDL seems to be quite strong, judged from affinity chromatography experiments. The studies did not reveal any interaction between SAA and albumin, and there was no evidence that SAA could complex to itself. By isolation of HDL apoproteins, SAA seems to behave like other known apoproteins and may he characterized as an apoprotein that is present in normal serum in very low concentration but increases in concentration under different unphysiological circumstances.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 5 (1976), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Human immune antibodies such as anti-Rh and anti-Kell antibodies were tested in hemagglutination and hemagglutination inhibition experiments for VH subgroup composition. A striking VH subgroup restriction was found in several of these groups of antibodies. In the majority of cases there was a restriction to one particular VH subgroup for a single antibody specificity in a given individual. In some cases there was also an overall restriction to one particular subgroup for antibodies with the same antibody specificity. This was particularly pronounced for anti-D antibodies, which were primarily restricted to VHII, and for the anti-Kell, which was particularly related to VHIII. Subgroup-specific antigens for all the main VH subgroups were blocked on combination of the antibody molecule with antigen. No relation was found between VH restriction and restriction to IgG subclass, or genetic markers or χ and λ light-chain type.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 5 (1976), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The Cγ2 homology region of rabbit IgG does not behave like a domain. Thus, there is no trans-interaction between the two Cγ2 regions: instead there is an unusual cis-interaction between Cγ2 and Cγ3 regions. The observations were made on the plasmin digestion products Facb (IgG minus the Cγ3 region) and pFc’(Cγ3 region), which did not dissociate under neutral conditions but dissociated in 3M guanidine solution (that is. cis-interaction between Cγ2 and Cγ3). The Facb fragment split into subunits with equal molecular weights under neutral conditions on partial reduction and alkylation (that is, lack of transinteraction between the two Cγ2 in the molecule).
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 5 (1976), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Four human sera with high titers of IgG anti-D were studied in recombination experiments with isolated heavy and light chains. The binding to the D antigen measured by hemagglutination with O,R1R2 erythrocytes was 30–60 times weaker isolated anti-D heavy chains and with hybrids of anti-D heavy chains and pooled light chains than with the parent anti-D IgG. Light chains and hybrids of light chains from anti-D IgG and pooled heavy chains showed no binding. This indicates that the heavy chains are more important in antigen binding than the light chains in this system. It was also shown that the idiotypes need both heavy and light chains of the anti-D molecule to give a positive reaction with specific anti-idiotypic antiserum.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 6 (1977), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: In the present study evidence is presented that SAA in serum complexes to a carrier protein with a molecular weight of 100,000–200,000 daltons, with mobility in the a-region on electrophoresis, and with a rather low normal strum concentration. The carrier protein is apparently not albumin. SAA isolated from the carrier protein has a molecular weight of 14,000 daltons and does not complex to any considerable extent with itself under neutral conditions.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 6 (1977), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Antisera specific for 4 different classes of amyloid fibril proteins, amyloid protein AA and the immunoglobulin light-chain amyloid proteins AλI, AλIV, and AλV, were used to identify these proteins directly in tissue sections from 25 patients with amyloidosis. The specificity of these reactions was established by blocking experiments with purified amyloid fibril proteins and Bence Jones proteins of known variable subgroups. Protein AA was detected in 17 patients, including all 13 with secondary amyloidosis, 2 with primary amyloidosis and 2 with Waldenström's macroglobulinemia. Immunoglobulin light-chain proteins Aλ I, AλIV, and Aλ V were found in 3, 1, and 2 patients, respectively, all of whom had primary or myeloma/macroglobulinemia-associated amyloidosis. Antiserum specific for the amyloid-related serum protein SAA reacted with the same tissues as anti-AA and had the same pattern of staining in tissue sections.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 6 (1977), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: In a series of experiments several idiotype-specific rabbit antisera produced against different IgG anti-Rh (D) antibodies reacted with other anti-Rh (D) antibodies and thus showed cross-idiotypic reactions. Some of the antisera agglutinated almost all types of anti-D-sensitized erythrocytes, whereas other idiotype-specific antisera agglutinated only a few anti-D-sensitized erythrocytes. Anti-D antibodies showed several different cross-idiotypic reaction patterns. The cross-idiotypic antigens were, in most instances, localized to the heavy chains only. In a few cases, however, the cross-idiotypic antigens were dependent on the interaction between heavy and light chains.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 9 (1979), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Antisera were raised against three polyclonal IgM rheumatoid factors (RF). After adequate absorptions, the antisera were rendered idiotype-specific, as assayed by haemagglutination technique. By using the anti-idiotype antisera in indirect immunofluorescence on peripheral blood lymphocytes from the patients used as donors for the immunizing RF, it was demonstrated that 3–14% of the lymphocytes were stained, and thus had membrane-bound structures with idiotypic antigens similar to those of the circulating IgM RF of the same patients. While most of these idiotype-positive lymphocytes were B lymphocytes, it was demonstrated in one patient that about 7% of the T lymphocytes also had the same idiotypic antigens.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 9 (1979), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Strong idiotypic antigens were detected both in monoclonal and polyclonal rheumatoid factors (RF) by applying idiotype-specific antisera. Shared idiotypic antigens were found between some polyclonal and monoclonal RF as well as between certain IgG and IgM RF.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 4 (1975), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Rabbit IgG anti-chicken erythrocyte antibodies were compared with the Fab/c or Facb fragments of IgG and with partially reduced and alkylated IgG for the capacity to induce cytotoxicity by normal human lymphocytes. The Fab/c antibody fragment, which lacks one Fab region, was still able to induce cytotoxicity. In contrast, the Facb antibody fragment, which lacks the Cγ3 domains, was nearly ineffective in activating the effector cells, whereas intact antibody activity was demonstrated by its ability to inhibit the cytotoxicity induced by unsplit IgG. Similarly, partial reduction and alkylation of the IgG antibodies, under conditions affecting the interchain disulphide bonds only, greatly diminished their ability to induce cytotoxicity, although they effectively inhibited the cytotoxicity induced by untreated IgG. On the basis of these results and previous data, we suggest that the reaction of the Fc region of IgG with the effector cell depends on the integrity of the Cγ2 domain in the native, divalent state or on the interaction between the Cγ2 and Cγ3 domains.
    Type of Medium: Electronic Resource
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