Electrophoretic, Ultracentrifugal, and Immunochemical Studies on Wassermann Antibody

Abstract

Summary Methods developed for dissociating Wassermann antibody from specific floccules by 15 per cent NaCl and ether or by alcohol and ether yielded preparations of as high as 87 per cent purity, as measured by the amount of protein removable by antigen. Serologic tests on serum fractions separated by electrophoresis, and electrophoretic analysis of a preparation of purified antibody, showed the Wassermann antibody to have a mobility intermediate between beta and gamma globulin. Ultracentrifugal concentration of whole syphilitic serum or electrophoretically separated gamma globulin showed a relative concentration of antibody in the sediment, indicating that a portion of the antibody has a higher molecular weight than the bulk of the globulin. Examination of purified antibody solutions showed that the antibody was associated with both a light and a heavy globulin component, of sedimentation constant 7 and 19 Svedbergs, respectively. The serologic titer of purified Wassermann antibody was nonspecifically increased 2 to 4 times by the addition of serum albumin or inactivated whole serum. Electrophoresis, ultracentrifugation, and purification of antibody failed to show significant differences between a number of syphilitic and false positive sera.