Abstract
The elucidation of the antigenic structures of human ceruloplasmin, fibrinogen, plasminogen, IgG, α1‐lipoproteins, β1C/A‐, and β1E‐globulins and–in continuation of earlier experiments–also of β‐lipoproteins and of prealbumin by use of the cross‐reactions between human and animal plasmas is reported. The experiments were done employing Ouchterlony's double diffusion technique in the micro‐modification. Absorption controls confirmed these results. The numbers of antigenic determinants with different specificities detected this way are: for ceruloplasmin: 3; for fibrinogen: 3; for plasminogen: 4; for IgG (γ‐chain only): 4; for α‐lipoproteins: 2; for β1C/A‐ and βE‐globulins: 2 each. Relations between the total number of determinants (including also determinants detectable by other methods only) and the chemical structure, especially the number of amino acid residues, are discussed in greater detail. The applicability of the technical approach to other problems of molecular immunology is described.
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