Abstract
The overall and internal structure of recombinant yeast-derived human hepatitis B virus surface antigen vaccine particles was investigated by small-angle neutron scattering using the contrast variation method. The vaccine is a nearly spherical particle, and its contrast-matching point was determined to be at about 24% D2O content, indicating that a large part of the vaccine particle is occupied by lipids and carbohydrates from the yeast. The Stuhrmann plot suggests that the surface antigens exist predominantly in the peripheral region of the particle, which is favorable to the induction of anti-virus antibodies.
Original language | English |
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Pages (from-to) | 757-759 |
Number of pages | 3 |
Journal | Physica B: Physics of Condensed Matter |
Volume | 213-214 |
Issue number | C |
DOIs | |
Publication status | Published - 1995 Aug 1 |
Externally published | Yes |
ASJC Scopus subject areas
- Electronic, Optical and Magnetic Materials
- Condensed Matter Physics
- Electrical and Electronic Engineering