Antibodies to enzymes--a tool in the study of antigenic specificity determinants.

Abstract

The study of antigenic specificity determinants has long been a subject of interest. Since the early studies of Landsteiner (1945) on the specificity of serological reactions and through numerous recent investigations with synthetic antigens (Sela, 1966) as well as protein conjugates (Boyd, 1962; Pressman and Grossberg, 1968), efforts have been aimed at the elucidation of the Structural features which are characteristic of the sites against which the antibodies are formed. Antibodies can be produced against the majority of enzymes can be employed, for example, in the search for enzymes of biological pathways which disappeared in the course of evolution, or to detect the extent of similarity between enzymes that persisted through the ages. In cases where the primary sequence of the enzymes is known, the elucidation of the immunological behaviour is feasible in precise molecular terms and should provide a sensitive probe of the surface conformation, in addition to the contribution in identifying antigenic determinants. The extensive studies on cytochrome c (e.g. Margoliash et al., 1967) have indeed demonstrated the power of this analytical approach. They demonstrated that antisera prepared against any one of several cytochromes c (the complete amino acid sequence of which is known) cross-react to a varying extent with the proteins from over 25 other species.