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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
    Heterogeneity of Degradation of B-Cell Endocytosed Monoclonal Antibodies Reacting with Different sIgM Epitopes (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 29 (1989), S. 0 
    Details
    ISSN: 1365-3083
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: The degradation of a panel of monoclonal antibodies (MoAb) bound to surface IgM (sIgM) was studied in three human Burkitt's lymphoma cell lines. The panel included MoAb that recognize several distinct epitopes associated with the F(cμ)5 domain, the cμ2 domain, and δ or λ light chains. The amount of degraded MoAb and the rate of their degradation varied considerably between the various antibodies. Properties of MoAb such as avidity or ability to cross-link sIgM did not significantly influence their degradation. The most consistent correlation between rate of degradation and MoAb used was the location of the epitope recognized by the individual MoAb. Thus, 7 out of 8 anti-light chain MoAb were degraded at a higher rate than 5 out of 5 anti-F(cμ)5 MoAb. One anti-cμ2 MoAb was degraded at a rate similar to the majority of anti-light chain MoAb. The intracellular transport of an anti-δ light chain MoAb and an anti-F(cμ)5 MoAb was studied in detail by subcellular fractionation in sucrose gradients. We found that the anti-δ light chain MoAb was transported more rapidly to lysosomes than the anti-F(cμ)5 MoAb, showing that they were sorted differently intracellularly.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-3083.1989.tb01128.x
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  • 5
    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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  • 6
    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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  • 7
    Digitale Medien
    Digitale Medien
    Monoclonal Human B Lymphoma Cells Respond by DNA Synthesis to Anti-Immunoglobulins in the Presence of the Tumour Promotor TPA (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 15 (1982), S. 0 
    Details
    ISSN: 1365-3083
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Monoclonal human B lymphoma cells were triggered in vitro to DNA synthesis with F(ab')2 fragments of rabbit IgG antibodies specific for different human immunoglobulin (Ig) light and heavy chains. The specificity of the responses corresponded to surface Ig (sIg) present on tumour cells. Anti-μ chain. anti-δ chain, anti-γ chain, and antibodies to light chains were found to mediate this effect. However, to induce DNA synthesis, the tumour promoter 12-O-tetradecanoyl-phorbol-13-acetatc (TPA) was usually required. TPA alone induced cytoplasmic protrusions and increases in cellular volume. These observations should provide new opportunities to study the triggering of B cells with anti-Ig in well-defined cell populations.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-3083.1982.tb00648.x
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  • 8
    Digitale Medien
    Digitale Medien
    Further Structural and Antigenic Studies of Light-chain Amyloid Proteins (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 14 (1981), S. 0 
    Details
    ISSN: 1365-3083
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: The major subunit protein of amyloid fibrils (758) isolated from a patient with systemic amyloidosis and studied by N-terminal amino acid sequence analysis was found to be almost identical to the sequence of a VλIV Bence-Jones protein and a previously described AλIV amyloid protein. The two AλIV amyloid proteins showed strong antigenic cross-reaction, appearing as antigenic identity in double immunodiffusion tests using anti-AλlV antiserum raised against one or the other of the two proteins. In addition, another new AλV amyloid fibril protein (R.S.) showed strong amino acid sequence homology and antigenic identity in double immunodiffusions with the prototype of the AλV subgroup (the AR protein). Finally, 20 primary or myeloma-associated amyloid proteins were characterized using antisera against the AA and several Ig light-chain-derived amyloid proteins.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-3083.1981.tb00187.x
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  • 9
    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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  • 10
    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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