Abstract
Recombinant yeast-derived human hepatitis B virus surface antigen vaccine particle was investigated by small-angle neutron scattering using contrast variation method. Contrast matching point of the particle was determined at 24% D2O content, indicating most of the non-protein components of the particle to be both lipids and hydrocarbons from yeast. However, the protein distribution is significantly different from that of lipids or hydrocarbons as indicated by the intensity profile difference at 40% D2O content solution from that of other D2O content solutions. The Stuhrmann plot is indicative of the fact that the antigenic protein is slightly dominant in the peripheral region of the spherical vaccine particle.
