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  • 1970-1974  (14)
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Year
  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 1 (1974), S. 0 
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: 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.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 3 (1974), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 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
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 3 (1974), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 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.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 1 (1972), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 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.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 1 (1972), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 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.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 190 (1971), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 3 (1974), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: An Fh fragment corresponding to the hinge region of IgG3 has been isolated by J single α-chymotrypsin treatment of whole IgG3 Various combinations of two enzymes have also been used, but with somewhat lower yield and less purity The isolated Fh fragment has features similar to those of the bound hinge region in the intact IgG3 and its F(ab')2 and Fch fragments. The Fh fragment has a char acteristically high content of cystine and proline and seems to lack aromatic amino acids
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 3 (1974), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Some human lymphocyte-like cells (EA-RFC) have receptors for IgG demonstrable by their ability to form rosettes with human Rh-positive O erythrocytes sensitized with anti-CD isoantibodies (Ripley). The specificity of these receptors for the various Ig classes, IgG subclasses, and fragments of the IgG molecule was determined by studying the inhibitory capacity of the corresponding immunoglobulins in the rosette assay. The receptors showed specificity only for IgG among the Ig classes and about equal affinity for IgG1 and IgG3, but only weak binding of IgG2 and IgG4 was obtained. Whereas no inhibition was obtained with Fab and F(ab')2 fragments prepared from IgG, the Fc fragment showed strong inhibitory capacity, which was even surpassed by the IgG3 Fch fragment, containing an extension from the N-terminal part of Fc. The inhibitory capacity of the Fc and Fch fragments was considerably reduced by partial reduction and alkylation. The pFc' fragment of IgG, which corresponds to the Cγ3 region, did not inhibit rosette formation. These data indicate that mainly the Cγ2 region is involved in the binding of IgG to EA-RFC. Inhibition studies did not show any differences in the relative inhibitory capacity of monomerie, dimeric, or highly polymerized (heat-aggregated) IgG. However, antibodies of rabbit origin complexed with antigen (ferritin) gave stronger inhibition than the corresponding native Ig.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 3 (1974), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: We present data concerning the mechanism of the binding of aggregated IgG and of IgG-sensitized erythrocytes by different human lymphocyte-like cells. The results showed that the two phenomena are related to different subpopulations of lymphocytes. By fractionation and depletion studies of B lymphocytes, T lymphocytes, and lymphocyte-like cells binding IgG-sensitized erythrocytes (EA-RFC), it was demonstrated that binding of aggregated IgG is related to B lymphocytes, whereas binding of IgG-sensitized erythrocytes depends on another subpopulation of lymphocyte-like cells. Whereas binding of IgG-sensitized erythrocytes by EA-RFCs depends entirely on the Fc fragment, binding studies with IgG fragments suggested that the interaction of aggregated IgG with B lymphocytes is different.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 3 (1974), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The cytotoxicity of human peripheral blood lymphocytes against chicken erythrocytes sensitized by rabbit antibodies was inhibited by human immunoglobulin and immunoglobulin fragments. Myeloma proteins isolated in dimeric state or aggregated by heat treatment inhibited better than the corresponding monomeric proteins. Strong inhibition was observed with IgG1 and IgG3, and with IgG2 after aggregation, while IgG4 inhibited very little. No inhibition was found with IgM, IgA. IgD and IgE. The F(ab')2. and Fab fragments of IgG inhibited poorly or not at all. While- considerable inhibition was observed with the Fc fragment, the pFc’ fragment, which roughly corresponds to the C-terminal half of the Fc portion, showed little inhibitory capacity. A fragment isolated from IgG3, containing an extension of the N-terminal part of Fc (the Fch fragment), was an even better inhibitor than tin Fc fragment. The inhibitory capacity of the Fch and Fc fragments was greatly diminished following partial reduction and alkylation On the basis of the inhibitory pattern of IgG fragments, it is suggested that the region on the immunoglobulin molecule involved in binding to the Fc receptor of the effector lymphocytic cell may be located within the CH2 domain.
    Type of Medium: Electronic Resource
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