1. Introduction. 2. The principle, history and use of bioaffinity chromatography. 3. Choice of affinity ligands (affinants). 4. General considerations on affinant - sorbent bonding. 5. Solid matrix supports. 6. Survey of the most common coupling procedures. 7. Characterization of supports and immobilized affinity ligands. 8. General considerations on sorption, elution and non-specific binding. 9. Bioaffinity chromatography in the isolation, determination or removal of biologically active substances. 10. Immobilization of enzymes by biospecific adsorption to immobilized monoclonal or polyclonal antibodies. 11. Study of the modification, mechanism of action and structure of biologically active substances using bioaffinity chromatography. 12. Solid-phase immunoassay and enzyme-linked lectin assay. 13. Several examples of the application of biospecific adsorption in medicine. 14. Application of bioaffinity chromatography to the quantitative evaluation of specific complexes. 15. Theory of bioaffinity chromatography. Subject Index.