[Studies of blood group antibodies. I. Fractionation of anti-A and anti-B Isohemagglutinins by anioncation cellulose exchange chromatography].

Abstract

Summary Through use of an anion exchange adsorbent, DEAE-cellulose, and a cation exchange adsorbent, CM-cellulose, isohemagglutinins anti-A and anti-B have been separated into three components. One fraction, of low anionic binding capacity, is associated with γ-2 globulins of low sedimentation constant. Its serologic behavior is characteristic of the “immune” antibody. A second fraction is of intermediate anionic binding capacity. It consists of an albumin-globulin mixture whose most conspicuous globulin component is α-2. The sedimentation constant (uncorrected) of the non-albumin portion of this fraction has been found to be 15.2. A third fraction is of high anionic binding capacity. It contains some non-γ-globulin and serologically-active γ-1 globulin. This γ-globulin is not homogeneous with respect to sedimentation constant. Serologically, the second and third fractions are similar in that they are not enhanced by high-protein diluents, but the third fraction contains relatively more hemolysin activity than the second.