ON HOMOGENEOUS ANTIGENS AND ANTIBODIES. III. THE PREPARATION AND PROPERTIES OF THE UNIVALENT HAPTEN‐PROTEIN CONJUGATE PAPAIN‐S‐DNPL*

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Abstract
SUMMARY: Karl Landsteiner's introduction of the systematic study of hapten‐protein conjugates and antihapten antibodies was a great milestone in immunology and immunochemistry. His work, and the work of others following his lead, have illuminated the character of the antigen‐antibody interaction, and have provided antibodies whose specificities could be systematically varied and used in a wide variety of structural studies. It is important to recognize, however, that while conventionally prepared hapten‐protein conjugates are extraordinarily useful as model antigens for certain types of immunochemical studies, they may not be as simple immunogens as has generally been assumed. An adequate appreciation of the two structural considerations: a) that antibody‐combining sites are, generally, considerably larger than simple haptenic groups; and b) that hydrophobic haptens will tend to be immobilized on patches of the surface of the carrier molecule, leads to the realization that from an antigenic point of view, hapten‐protein conjugates may be, in fact, at least as complex and heterogeneous as are protein antigens themselves. Studies with such conjugates that ignore their complexities may come to erroneous conclusions about important immunological phenomena. The use of less heterogeneous or homogeneous hapten conjugates in these experiments may avoid, or at least minimize, such difficulties, and may also lead to the production of homogeneous antibodies useful for detailed chemical and structural studies.