TY - JOUR
T1 - Small-angle neutron scattering study of recombinant yeast-derived human hepatitis B virus surface antigen vaccine particle
AU - Sato, M.
AU - Ito, Y.
AU - Kameyama, K.
AU - Imai, M.
AU - Ishikawa, N.
AU - Takagi, T.
PY - 1995/8/1
Y1 - 1995/8/1
N2 - 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.
AB - 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.
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U2 - 10.1016/0921-4526(95)00271-A
DO - 10.1016/0921-4526(95)00271-A
M3 - Article
AN - SCOPUS:0029354740
SN - 0921-4526
VL - 213-214
SP - 757
EP - 759
JO - Physica B: Condensed Matter
JF - Physica B: Condensed Matter
IS - C
ER -
