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  • 1
    Digitale Medien
    Digitale Medien
    IgG1 SUBCLASS PROTEIN WITH THE GENETIC Gm MARKERS Gm(z + non-a +): ANOTHER EXAMPLE OF INTRAGENIC HYBRIDIZATION AMONG IgG SUBCLASS GENES (1974)
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 1 (1974), S. 0 
    Details
    ISSN: 1744-313X
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie , Medizin
    Notizen: A new type of Gm genetic marker combination in an IgG1 immunoglobulin, Gm(z) together with a non-a marker, is here described. This indicates the presence of a new gene, Gmz,non-a, which most likely originated on the basis of an intragenic recombination at the IgG1 cistron. Immunochemical and immunogenetic studies showed that no other IgG1 Gm markers were expressed by the unusual gene, and there was no evidence for deletions or duplications at the IgG1 cistron.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1744-313X.1974.tb00288.x
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  • 2
    Digitale Medien
    Digitale Medien
    Same Idiotypc of B-Lymphocyte Membrane IgD and IgM. Formal Evidence for Monoclonality of Chronic Lymphocytic Leukemia Cells (1974)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 3 (1974), S. 0 
    Details
    ISSN: 1365-3083
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Idiotypic antisera were raised in rabbits against serum M-cnmponents in two patients with chronic lymphocytic leukemia (CLL) In one of the patients the leukemic cells had membrane-bound IgG. in the other IgM and IgD. The M-components were IgG and IgM. respectively. By immunofluorescence technique the CLL cells were shown to be positive when stained with idiotypic antiserum prepared against the corresponding M component, whereas normal lymphocytes, as well as cells from other CLL patients, were negative. These findings represent strong evidence for the monoclonality of the malignant B cells in CLL The fact that the CLL cells had membrane-bound Ig with the same idiotypic determinants as the corresponding serum M-component indicated that the latter had been synthesized and secreted by the malignant clone of B cells. In further experiments redistribution of membrane-bound Ig on CLL cells bearing both IgM and IgD was induced with idiotypic antiserum This indicated that IgM and IgD on the same cells share idiotypic specificity and therefore have the same variable region and. presumably, the same antibody specificity
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-3083.1974.tb01321.x
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  • 3
    Digitale Medien
    Digitale Medien
    Comparison of Fch and Fc Fragments of IgG3: Evidence of an Intra-Chain S-S Bridge in the Hinge of γ3 Chains (1974)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 3 (1974), S. 0 
    Details
    ISSN: 1365-3083
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: The Fc and Fch fragments of human IgG3, appearing late and early during papain digestion, respectively, were antigenically and structurally compared. Only the Fch fragment reacted with an anti-Fh (hinge region-specific) antiserum; thus the main portion of the hinge region is split off during the formation of Fc fragments The Fch fragment has a higher content of inter-chain S-S bridges than the Fc fragments. The Fc fragments are probably a mixture of three related fragments. The Fch fragment appears to be more homogeneous, although there was hydrolysis at the C-terminal site of the hinge region in some of the Fch chains. Evidence is presented that the γ3 chain bridge has an extra intra-heavy-chain disulphidc bridge at the C-terminal end of the hinge region.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-3083.1974.tb01325.x
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  • 4
    Digitale Medien
    Digitale Medien
    Antigenic and Chemical Characterization of Non-Immunoglobulin Amyloid Proteins (1972)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 1 (1972), S. 0 
    Details
    ISSN: 1365-3083
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: The results of antigenic and chemical studies on subcomponents of amyloid fibrils secondary to chronic inflammatory diseases are reported. Treatment of amyloid with either guanidine and dithiothreitol or sodium hydroxide followed by gel filtration on Sephadex G-100 revealed two major protein components, one eluted in the void volume (m. w. 〉200, 000), the other having an m. w. of 5, 000. Results from amino acid composition and N-terminal sequences and also antigenic analysis suggest that the components are two different proteins not related to immunoglobulins.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-3083.1972.tb03305.x
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  • 5
    Digitale Medien
    Digitale Medien
    Three New Fragments, F(ab)2, F(c)2, and Fab/c, Obtained by Papain Proteolysis of Normal Human IgG. (1972)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 1 (1972), S. 0 
    Details
    ISSN: 1365-3083
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Three new fragments, each with a molecular weight of about 100,000, were isolated after papain proteolysis of normal monomer human IgG. The fragments isolated were as follows: F(c)2 fragment with Fc determinants only, Fab/c fragment with both Fc and Fab determinants, and F(ab′) fragment with only Fab determinants. The F(c)2 fragment appeared to be a dimer of Fc stabilized by disulphide bonds, whilst the F(ab)2 fragment consisted of Fab subunits mainly held together by non-covalent forces. The Fab/c fragment is probably a single Fab fragment and the Fc fragment held together by an unbroken heavy chain.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-3083.1972.tb01817.x
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  • 6
    Digitale Medien
    Digitale Medien
    High-Density Lipoprotein as Carrier for Amyloid-related Protein SAA in Rabbit Serum (1979)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 10 (1979), S. 0 
    Details
    ISSN: 1365-3083
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-3083.1979.tb01332.x
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  • 7
    Digitale Medien
    Digitale Medien
    Restriction of Human Immune Antibodies to Heavy-Chain Variable Subgroups (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 5 (1976), S. 0 
    Details
    ISSN: 1365-3083
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-3083.1976.tb03016.x
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  • 8
    Digitale Medien
    Digitale Medien
    Indications That the Cγ2 Homology Region Is Not a Regular Domain (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 5 (1976), S. 0 
    Details
    ISSN: 1365-3083
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: 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).
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-3083.1976.tb00253.x
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  • 9
    Digitale Medien
    Digitale Medien
    Antibody Activity of Heavy and Light Chains and Recombined IgG of Human IgG Anti-D (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 5 (1976), S. 0 
    Details
    ISSN: 1365-3083
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-3083.1976.tb03002.x
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  • 10
    Digitale Medien
    Digitale Medien
    Comparison of Surface Properties of Human IgA, IgE, IgG and IgM Antibodies with Identical and Different Specificities (1996)
    Oxford, U.K. and Cambridge, USA : Blackwell Science Ltd
    Scandinavian journal of immunology 44 (1996), S. 0 
    Details
    ISSN: 1365-3083
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: In this paper, the authors report the use of liquid-liquid partition chromatography (LLPC) in an aqueous polyethylene glycol (PEG)/dextran two-phase system to compare the surface properties (partition properties) of human antibodies and fragments thereof. The surface properties of all the monoclonal antibodies of different classes and subclasses investigated were within the same broad range as that observed for the polyclonal antibodies and no relationship was found between the exposed surfaces of the immunoglobulins (Ig) and their heavy chain isotype. Moreover, Fc fragments from various IgG1, 2 and 4 myeloma proteins were found to exhibit similar surface properties. Employing chimeric antibodies with identical variable regions the authors found that intact IgG1, 2 and 4 displayed identical surface properties, while the corresponding IgA1, IgA2, IgG3, IgE and IgM antibodies differed both from each other and from the IgGs. The surface properties of chimeric IgG3 could be made similar to those of the IgG1, 2 and 4 chimers by partially reducing the length of the hinge section, but new differences in surface properties appeared when their hinges were of similar length. Thus, LLPC can be used to detect differences or similarities in the surface properties of the antigen-binding regions as well as the Fc part in the various isotypes. This can shed light on biological activities such as antigen binding and effector function.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1046/j.1365-3083.1996.d01-329.x
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