Biophysical and biochemical properties of purified preparations of hepatitis B surface antigen (HBs Ag)

Abstract

Two antigenically distinct subtypes, adw and ayw, of hepatitis B surface antigen (HBs Ag), have been purified from the plasma of anicteric hepatitis patients. Biophysical studies of these purified preparations revealed considerable heterogeneity in their overall surface charge, morphology and molecular weights. Chemical studies revealed that the composition of the particles is complex in that four to six different polypeptides and three glycoproteins were identified. In addition, cholesterol, three polar lipids, and two glycolipids were detected in purified HBs Ag preparations. Antisera, prepared in guinea pigs to individual polypeptides derived from HBs Ag subtypes adw and ayw, reacted with both the group- and type-specific antigenic determinants associated with the intact particles. The potential of these purified preparations of HBs Ag and of the individual subunits derived from them as possible vaccines is discussed. Specific antipolypeptide sera will be utilized to determine whether HBs Ag components are synthesized as specific viral products or are composed of components of modified host-cell molecules.