Antisera to a peptide representing the extreme carboxy terminus of the hepatitis delta virus antigen (HDAg) open reading frame (residues 197 to 211) recognized only the large (p27) and not the small (p24) form of HDAg in immunoblots of infected liver extracts, thereby providing direct proof that p27 and p24 differ in their carboxyl-terminal sequence and that p27 results from mutation within the stop codon terminating translation of p24. Reactions with other peptide antisera demonstrated that multiple smaller virus-specified proteins were carboxy-terminally truncated forms of HDAg, and immunoprecipitation studies suggested that different forms of HDAg were present as heterologous complexes within the liver extract.


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