| Abstract: | Reduction and alkylation of purified hepatitis-associated Australia antigen (hepatitis B antigen) resulted in a total loss of serologic activity. The reduced and alkylated protein formed a single band with a sedimentation coefficient of 31S on analytical ultracentrifugation, and no subunits were detected by Sephadex gel filtration. Although this preparation induced a delayed hypersensitivity response when injected into guinea pigs, it failed to stimulate humoral antibody formation. The data suggest that hepatitis B antigen is a conformational antigen critically dependent upon the disulfide bonds of the protein moiety. |
