Generation and Measurement of Antibodies

  • H. F. J. Savelkoul
  • S. S. Pathak
  • N. R. Sabbele
  • R. Benner
Part of the Handbook of Experimental Pharmacology book series (HEP, volume 85)

Abstract

The antibody (Ab) molecule has evolved to perform two distinct functions: epitope recognition and elimination of foreign antigens (Ag). Ab activity resides in immunoglobulin (Ig) molecules, each of which can interact with some of a virtually unlimited number of physicochemically different Ags. These Ags include exogenous (foreign or nonself) as well as endogenous (self) Ags, including Ig idiotopes (Eichmann 1978; Jerne 1984; Köhler et al. 1984). In spite of the large variety of different Ab specificities, Ab destroy or eliminate foreign Ag by a small number of effector mechanisms. To carry out its dual function, the Ab molecule has evolved discrete globular domains: one of these domains binds Ag, whereas the others mediate effector mechanisms (Edelman 1973). Thus, the functional duality of the Ab molecule is reflected in its three-dimensional structure. The organization of Ab-gene clusters also reflects this duality (Honjo 1983; Calvert et al. 1984).

Keywords

Cholesterol Surfactant Manifold Titration Polystyrene 

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Copyright information

© Springer-Verlag Berlin Heidelberg 1988

Authors and Affiliations

  • H. F. J. Savelkoul
  • S. S. Pathak
  • N. R. Sabbele
  • R. Benner

There are no affiliations available

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