Interaction between polyalbumin and pre-S2 region of hepatitis B surface antigen does not require the whole native structure of human serum albumin

Abstract

Human serum albumin was treated with glutaraldehyde and the modified products were separated by size into three species: monomer, dimer and polymer. All the species produced from native human serum albumin bound to pre-S2 region (120-174) of hepatitis B virus surface antigen. The same was true of three modified species which were derived from the denatured human serum albumin. Receptor-ligand immunoblotting of human serum albumin cleaved by cyanogen bromide and fixed by glutaraldehyde indicated that binding of pre-S2 to polyalbumin could be confined to at least three segments (amino acids 124-297, 329-445 and 446-547) of human serum albumin.