Abstract
An unique component polypeptide (MW 49000 dalton) bearing all of the known antigenic determinants (a, Re, d, and r) was isolated by treatment with sodium dodecyl sulfate, gel filtration, and SDS polyacrylamide gel electrophoresis of purified 22-nm particles from HBV (adr) infected human plasma pool. This polypeptide, designated as p-49, splitted into two smaller polypeptides of different molecular weight-22000 (p-22) and 27000 dalton (p-27)by reduction with 2-mercaptoethanol. p-27 and p-49 were glycoproteins. The antigenicity assayed by reversed passive haemagglutination or haemagglutination inhibition and the immunogenicity tested by injection to mice of p-49 were almost same as 22-nm particles, although significantly superior to the two major component polypeptides-p-22 and p-27.
