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  • The American Association of Immunologists  (4)
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  • The American Association of Immunologists  (4)
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  • 1
    Online Resource
    Online Resource
    The American Association of Immunologists ; 1947
    In:  The Journal of Immunology Vol. 55, No. 2 ( 1947-02-01), p. 153-160
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 55, No. 2 ( 1947-02-01), p. 153-160
    Abstract: Washed Wadsworth-Brown floccules, presumably consisting of lipoid antigens in combination with syphilitic antibody, evoke in rabbits two different antibodies, one against the lipoid antigen, the other against syphilitic antibody. Rabbit anti-syphilitic-antibody reacts equally well, and with high dilutions, with both normal and syphilitic human serum. It reacts with the total globulin fraction of normal serum to the same titer as with whole serum, and with water-insoluble globulin to an only slightly lower titer. The water-soluble globulin gives reaction only in 8 to 10 times higher concentration, and the albumin in 1000 times higher concentration. The specificity of syphilitic antibody seems to be the same as that of certain normal serum globulins. It seems to be more closely related to the euglobulin fraction than to the pseudoglobulin.
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    RVK:
    RVK:
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 1947
    detail.hit.zdb_id: 1475085-5
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  • 2
    Online Resource
    Online Resource
    The American Association of Immunologists ; 1941
    In:  The Journal of Immunology Vol. 42, No. 2 ( 1941-10-01), p. 181-186
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 42, No. 2 ( 1941-10-01), p. 181-186
    Abstract: By combination of hemolytic streptococcal protein with an azo component and study of the chemical and serological properties of the resulting red azo antigen it is shown that only a portion of the azo-protein reacts serologically. An antiserum to the dye-streptococcal protein contained anti-hapten since it precipitated its red analogs, R-salt-azobiphenylazo egg albumin and R-salt-azo-biphenylazo-horse serum albumin.
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    RVK:
    RVK:
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 1941
    detail.hit.zdb_id: 1475085-5
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  • 3
    Online Resource
    Online Resource
    The American Association of Immunologists ; 1941
    In:  The Journal of Immunology Vol. 42, No. 2 ( 1941-10-01), p. 187-198
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 42, No. 2 ( 1941-10-01), p. 187-198
    Abstract: Proteic fractions were isolated from a type 1 strain of hemolytic streptococcus by grinding and extracting undried cells in the cold. One of the most active fractions was sub-fractionated by means of sodium chloride. The serological activity of the fractions was determined by quantitative precipitin-tests. Tryptic digestion of streptococcal proteins indicated the serological activity to be in large part due to difficultly digestible or possibly non-proteic components which appear to be major antigens or haptens of the cell. The presence of C-substance in protein and protein-digest fractions was regularly encountered and its importance in the reactivity of fractions toward antisera emphasized.
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    RVK:
    RVK:
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 1941
    detail.hit.zdb_id: 1475085-5
    Location Call Number Limitation Availability
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  • 4
    Online Resource
    Online Resource
    The American Association of Immunologists ; 1949
    In:  The Journal of Immunology Vol. 62, No. 3 ( 1949-07-01), p. 271-276
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 62, No. 3 ( 1949-07-01), p. 271-276
    Abstract: Two mucoid, inagglutinable strains of Escherichia coli were found to be almost as reactive as the capsule-free forms in respect of their capacity to bind complement and to absorb antibody. A study by means of titrations of agglutinins and complement fixing antibodies, and by quantitative agglutinin determinations, showed that the inagglutinability of these two strains must be due to inhibition of aggregate formation and not to reduced combining power.
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    RVK:
    RVK:
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 1949
    detail.hit.zdb_id: 1475085-5
    Location Call Number Limitation Availability
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