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  • 1
    Electronic Resource
    Electronic Resource
    Duplication of J κ genes within genus Rattus (1987)
    Springer
    Immunogenetics 26 (1987), S. 14-20 
    Details
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract We have isolated a region containing the immunoglobulin kappa chain joining segments from a liver DNA library of the Australian rat Rattus villosissimus, and determined its nucleotide sequence. While the laboratory rat (Rattus norvegicus) had previously been shown to contain three recently duplicated copies of J κ 2, R. villosissimus has only two. Furthermore, all three copies of J κ 2 in R. norvegicus share an 11 by deletion in their 5′ flanking regions which is not evident in either copy of J κ 2 in R. villosissimus. This suggests that the initial duplication events occurred separately in the two lineages, and were followed by a second duplication in R. norvegicus, all three duplications having occurred within the last 6–12 million years (although more complicated schemes involving gene conversion events cannot be excluded). These results indicate that there is a high degree of plasticity in this region of the genome, and that selective forces must exist which have maintained the number of expressible J κ segments in humans (5) and rodents (4–6) within their narrow range.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00345449
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  • 2
    Electronic Resource
    Electronic Resource
    EXPRESSION OF IMMUNOGLOBULIN LAMBDA CHAINS IN THE LABORATORY RAT (1986)
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 13 (1986), S. 0 
    Details
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: We immunized a BALB/c mouse with the lambda-bearing rat IgG, myeloma IR31, fused its spleen cells with the hybridoma parent line P3.X63.Ag8.653, and isolated a monoclonal antibody (G33/11) directed against rat immunoglobulin lambda chains. We used this antibody to classify two existing rat hybridomas as lambda-bearing proteins (D4.37HL.252 and PC61.5, and isolated one new lambda-bearing rat IgM hybridoma, G36/1. All the normal inbred rat sera that were tested contained lambda-bearing Ig as detected by G33/11, at levels ranging from 1.5% to 13% of the total serum Ig, the mean value being 7.9%. This antibody will be valuable for broadening our understanding of the immunogenetics of the rat, and for the characterization of monoclonal antibodies made in this species.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1744-313X.1986.tb01114.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    The Binding of Murine IgM to Staphylococcal A Protein (1978)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 7 (1978), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The binding of Staph A protein to murine immunoglobulins has previously been thought to be restricted to the IgG2 and IgG3 classes. In this study five IgM proteins were assessed for binding, and of these one showed marked Staph A binding. Pepsin digestion of this IgM molecule produced several different sized fragments, and the binding studies with these fragments indicated that the binding site is in the CH2 domain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1978.tb00466.x
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    Paper (German National Licenses)
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