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Antibodies from syphilitic sera have been studied by ultracentrifugation (Davis, Moore, Kabat, and Harris, 1945; Aho, 1967), paper electrophoresis (Laurell, 1955), immunoelectrophoresis (N0rredam and Clausen, 1963), gel diffusion (Laurell, Oxelius, and Rorsman, 1968), or by DEAE cellulose column chromatography (Laurell and Malmquist, 1961), and gel filtration on Sephadex G-200 (Julian, Logan and Norins, 1969). The immunoglobulin classes in sera of patients with late syphilis have been studied using monospecific fluorescent antisera (Logan, Norins, Atwood, and Miller, 1969). Immunoglobulin sequence has also been studied. Different results were obtained, however, and because these methods are time-consuming only a few sera were examined. It is generally accepted that the two most important classes of immunoglobulins differ in sedimentation characteristics as well as in their sensitivity to disulphide bond-reducing agents. Immunoglobulins of one class have sedimentation rates of 7S and the second class of immunoglobulins have sedimentation rates of 19S. The latter are more sensitive to disulphide bond-reducing compounds, dissociating into smaller subunits and losing the capacity to combine with antigen after such treatment. The same procedure is ineffective with antibodies of the 7S class and the two classes can therefore be easily differentiated by 2-mercaptoethanol treatment. We have made a study of the sulphydryl sensitivity of syphilitic antibodies, and have also investigated the temperature dependence of2-mercaptoethanol treated and untreated sera in complement fixation, to determine whether they fix complement more efficiently at 4°C. or at 37°C. Cunniff and Stollar (1968) established with several antigen-antibody systems the temperature dependence of complement-fixing capacity. They found that 7S antibodies reacted much more efficiently at 37°C. than at 4°C. and that 19S antibodies fix complement better at 37°C. We have tried to discover how far the observations of Cunniff

Sulphydryl sensitivity of syphilitic antibodies and temperature dependence in complement fixation.