Abstract
The synthesis of the hepatitis B surface antigen (HBsAG) in cells of Saccharomyces cerevisiae and its subsequent isolation, purification and analysis is described. The final, purified HBsAg particle exhibits close structural and biochemical similarities to particles derived from the plasma of chronically infected humans. Particles of yeast and human origin have been found, by chimpanzee efficacy studies and by various in vitro analyses, to be immunologically equivalent. The antigenic expression of a determinant-specific epitopes, as measured by antibody binding to synthetic peptides, has also been shown to be equivalent.
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