Abstract
The structural polypeptides of HBsAg were shown to be immunogenic in guinea pigs. Purified 22-nm forms of the ad and ay subtypes of HBsAg were solubilized under reducing conditions and electrophoresed in SDS-polyacrylamide gels. Individual polypeptides isolated from both HBsAg/ad and HBsAg/ay subtypes were used to hyperimmunize guinea pigs using Freund's complete adjuvant. All antimals produced specific antibodies against native HBsAg as determined by complement fixation, passive hemagglutination, and double-antibody radioimmunoprecipitation assays. Each polypeptide contained within its structure the group-specific HBsAg determinant, a. Equilibrium competitive inhibition studies were conducted to determine the relative affinities of antisera produced against the major HBsAg polypeptides P-1, P-2, and P-6 (23,000, 29,000, and 72,000 daltons, respectively.)
Footnotes
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↵1 The Rockville Laboratory of the MAN Program is supported by the NIAID under Union Carbide's contract with the United States Energy Research and Development Administration.
- Received March 31, 1975.
- Copyright © 1975 by The American Association of Immunologists, Inc.
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