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  • 1
    Electronic Resource
    Electronic Resource
    Comparison of the Cytoplasmic Antigens of Leprosy-Derived Corynebacteria and Some Mycobacteria (1983)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 17 (1983), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The immunological relationship between leprosy-derived corynebacteria (LDC) and reference mycobacteria was analysed by crossed immunoelectrophoresis with intermediate gel. For this purpose, three reference systems (LDC15/anti-LDC15, LDC18/anti-LDC8, and LDC8/anti-LDC8) were developed. They showed 15 to 20 distinct antigenic components in LDC cytoplasm. Extensive cross-reactivity was observed among different LDC isolates, affecting 3 to 17 components. Moreover, several components were shown to cross-react with mycobacteria when anti-bacillus Calmette-Gudrin (BCG), anti-Mycobarterium leprae, other antisera and lepromatous leprosy sera were incorporated in the intermediate gel. The major cross-reactive component, antigen M, was present in all LDC isolates and cross-reacted with antigen 7 of M. leprae and antigen 60 of M. bovis BCG. The thermostability of these antigens and the specificity of the cross-reacting antigens were assessed. The data underline the degree of immunochemical homogeneity within the LDC group of microorganisms and relatedness with M. leprae and other mycobacteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1983.tb00817.x
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  • 2
    Electronic Resource
    Electronic Resource
    Oligoclonal Macroglobulinaemia (1972)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 1 (1972), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Ninety macroglobulinaemia sera were tested for occurrence of multiple mono clonal immunoglobulins. Thirteen (14%) of the sera contained more than one monoclonal immunoglobulin. The homogeneous macroglobulins were isolated from 3 sera; in each case individually specific antigenic determinants common to the two components were demonstrated, in addition to determinants unique for each component. NH2-terminal amino acid sequence studies in two pa tients showed that the IgM heterogeneity was due to differences in the primary structure of the variable parts of the x (case To) and the μ (case Nae) chains. Macroglobulinaemia appears to be a unique source of homogeneous immuno-globulins from related clones.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1972.00019.pp.x
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  • 3
    Electronic Resource
    Electronic Resource
    Oligoclonal Macroglobulinaemia (1972)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 1 (1972), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Ninety macroglobulinaemia sera were tested for occurrence of multiple monoclonal immunoglobulins. Thirteen (14%) of the sera contained more than one monoclonal immunoglobulin. The homogeneous macroglobulins were isolated from 3 sera; in each case individually specific antigenic determinants common to the two components were demonstrated, in addition to determinants unique for each component. NH2-terminal amino acid sequence studies in two patients showed that the IgM heterogeneity was due to differences in the primary structure of the variable parts of the μ (case Tö) and the μ (case æ) chains. Macroglobulinaemia appears to be a unique source of homogeneous immunoglobulins from related clones.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1972.tb03731.x
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  • 4
    Electronic Resource
    Electronic Resource
    Heterogenous Expression of the Related MBP70 and MPB83 Proteins Distinguish Various Substrains of Mycobacterium bovis BCG and Mycobacterium tuberculosis H37Rv (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: MPB70 and MPB83 are homologous cross-reactive secreted mycobacterial proteins with very limited species distribution. The expression of these two proteins was compared between several substrains of Mycobacterium bovis BCG, virulent M. bovis and Mycobacterium tuberculosis H37Rv. A polyclonal antibody specific for MPB70 in Western blotting, and a monoclonal antibody, MBS43, found to be specific for MPB83 in ELISA and Western blotting, were used for the comparison. The previously established pattern of high- and low-producing substrains of BCG for MPB70 is only partially applicable for MPB83. MPB70 low-producing strains are also MPB83 low-producing, but the expression of MPB83 is much more variable than the expression of MPB70 in the MPB70 high-producing strains. Purified MPB83 (23 kDa) was found to be glycosylated. A band in SDS-PAGE at 1–2 kDa lower than that of purified MPB83 may represent unglycosylated MPB83. Furthermore, it was confirmed that purified MPB70 (22 kDa) is unglycosylated. There is cross-reactive antigen at 26 kDa. The MPB83 related antigen at 26 kDa was found to be the most abundant. These findings indicate greater heterogeneity between different substrains of BCG than previously realized. Virulent M. bovis produce and secrete large amounts of MPB70 and MPB83 while both these proteins occur in a far lower concentration in M. tuberculosis
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-3083.1996.d01-61.x
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  • 5
    Electronic Resource
    Electronic Resource
    Protein A Reactivity of Two Distinct Groups of Human Monoclonal IgM (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: Fifteen human monoclonal IgM proteins could be divided into two groups based on their ability to inhibit binding of a labelled human monoclonal IgM (IgM-Se) to Staphylococcus aureus Cowan 1 (IgM-Se assay); seven were positive and eight were negative. We found complete agreement between positive reaction in the IgM-Se assay, the presence of protein A reactivity in gel diffusion experiments, and high litres in an indirect haemagglutination test that detects antibodies to protein A—IgG complexes. The protein A precipitation patterns of IgM and autologous IgG were not identical.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1975.tb03726.x
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  • 6
    Electronic Resource
    Electronic Resource
    Protein A Reactivity of Two Distinct Groups of Human Monoclonal IgM (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: Fifteen human monoclonal IgM proteins could be divided into two groups based on their ability to inhibit binding of a labelled human monoclonal IgM (IgM-Se) to Staphylococcus aureus Cowan 1 (IgM-Se assay); seven were positive and eight were negative. We found complete agreement between positive reaction in the IgM-Se assay, the presence of protein A reactivity in gel diffusion experiments, and high titres in an indirect haemagglutination test that detects antibodies to protein A-IgG complexes. The protein A precipitation patterns of IgM and autologous IgG were not identical.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1975.tb02695.x
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  • 7
    Electronic Resource
    Electronic Resource
    Common Idiotypic Antigenic Determinants on Monomeric (7S) and Polymeric IgM from the Same Serum (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: Polymeric and monomeric IgM (7S IgM) were obtained from the serum of two patients with Waldenström's macroglobulinemia. The polymeric IgM was used for immunization of rabbits After absorption with unrelated IgM, eight antisera precipitated with the immunizing antigen but did not react with other polymeric IgM proteins The antisera thus disclosed idiotypic antigenic determinants. The precipitate formed between an antiserum and polymeric IgM could be completely inhibited by 7S IgM from the same scrum in double diffusion tests in agarose gels, although only one of the eight antisera precipitated with 7S IgM The reaction of Fabμ and various types of subunits (IgMs) from polymeric IgM with the antisera was also tested The findings arc compatible with the assumption that 7S IgM and polymeric IgM have identical idiotypic antigenic determinants, although the possibility that minor differences exist cannot be excluded.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1975.tb02664.x
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  • 8
    Electronic Resource
    Electronic Resource
    Immunohistochemical Detection of the Membrane and Fluid-phase Terminal Complement Complexes C5b-9(m) and SC5b-9 (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 26 (1987), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Activation of the terminal pathway of complement on a membrane results in the generation of the membrane-damaging terminal C5b-9(m) complement complex, whereas the non-lytic water-soluble SC5b-9 complex is formed when complement is activated in the fluid phase. Both forms of the terminal complement complex (TCC) can be immunohistochemically detected. but not distinguished, by antibodies recognizing neoantigens in the complexes. By means of monoclonal antibodies against C9 neoantigens and against the S-protein. it was demonstrated that deposits of the TCC in tissue sections may be either in the form of C5b-9(m) or SC5b-9. The consequences of this for the interpretation of the histochemical data and the terminology of the two complexes are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1987.tb02270.x
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  • 9
    Electronic Resource
    Electronic Resource
    Analysis of Monoclonal Antibodies to Mycobacterium leprae by Crossed Immunoelectrophoresis (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 25 (1987), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Monoclonal antibodies to Mycobacterium leprae were characterized in crossed immunoelectrophoresis and showed markedly different patterns of reactivity with M. leprae lines 2, 7 and 11 respectively. Line 7 corresponds to a cell wall-associated macromolecular complex containing lipid, polysaccharide, and two distinct 36 K and 65 K proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1987.tb01056.x
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  • 10
    Electronic Resource
    Electronic Resource
    7S Immunoglobulin M (IgM) from Serum Purified by Anti- μ -Chain 522 (1973)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 2 (1973), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Purification of 7S IgM from the serum of a patient with Waldenström's macro glubulinaemia by means of gel filtration and elution from an anti-μ-chain immunoadsorbent is described. Reduction of pure 7S IgM with 2-mercaptoethanol followed by removal of the reducing agent increased slightly the sedimentation in the ultracentrifuge of a fraction of the molecules. By contrast, when I9S IgM and a small amount of 125I-labelled 7S IgM were similarly treated together, a large fraction of the iodine-labelled material sedimented with the reassociated I9S IgM. The reassociation properties of purified alkylated and non-alkylated IgM subunits made by reduction of I9S IgM with 0.2 M mercaptoethanol or 0.02 M cysteine were analysed as described for 7S IgM.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1973.tb02057.x
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