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  • 1980-1984  (3)
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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 10 (1983), S. 0 
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 8 (1981), S. 0 
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Haemagglutination inhibition studies using isolated membrane components from rat red blood cells showed that the activity of the major antigenic system RT2 was contained exclusively in the glycoprotein fraction and confirmed immunochemically the existence of two alleles, RT2a and RT2b. The SDS-PAGE analysis of the membrane showed two interconvertible glycoproteins of apparent molecular weight 72,000 and 36,000, and the higher molecular weight component appeared to be a dimer of the lower molecular weight one. Analysis of the various membrane preparations after 125I-labelling showed that the glycoproteins existed in at least two molecular species on the surface of the red cells and that one species was more readily radio-iodinated and dimerized than the other. The RT2 antigenic specificities were preferentially associated with this component.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 10 (1983), S. 0 
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Five monoclonal antibodies reacting with class I MHC antigens were produced by fusing lymphocytes from WF (RT1u) rats immunized against DA (RT1a) rats with P3-X63-Ag8-653 myeloma cells. Sequential immunoprecipitation studies with the mAb and the WF anti-DA alloantiserum demonstrated the presence of four different class I molecules: all four molecules were reactive with the alloantiserum; three of them contained the determinant for mAb 155; two of the latter three molecules shared the determinants for mAb 3, 56 and 60, and one of these two molecules also contained the determinant for mAb 118. The four molecules could be isolated from the antigen preparation by sequential immunodepletion first with 118, next with 3, then with 155 and finally with the alloantiserum or by sequential absorption with affinity columns of Sepharose 4B coupled to the antibodies. The three antigens which were sequentially isolated with the mAb 118, 3, and 155, respectively, were analysed by SDS-PAGE after digestion with Staphylococcus aureus V8 protease, and they showed differences in peptide patterns. The relative amounts of the antigens expressed on red blood cells and on lymphocytes were different based on the results of sequential isolation and indirect cellular radioimmunoassay: the antigen which reacted with both mAb 3 (and 56 or 60) and 155 was the major class I antigen on red blood cells, and the antigen which reacted with mAb 118, 3 (and 56 or 60) and 155 was the major class I antigen on lymphocytes.
    Type of Medium: Electronic Resource
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