JaLCDOI 10.18926/AMO/32216
フルテキストURL fulltext.pdf
著者 Konobe, Takeo| Ishikawa, Nobuyoshi| Gohda, Hideo| Fukai, Konosuke| Okabe, Akinobu|
抄録 <p>The hepatitis B virus surface antigen containing the preS2 nine amino acid sequence produced by a recombinant Saccharomyces cerevisiae (yHBsAg) was purified and its physicochemical properties were determined. Ultrastructurally, the yHBsAg was found to be a homogeneous spherical particle with a diameter of 24 +/- 4 nm. The homogeneity of the yHBsAg particles was also demonstrated by analyses of their buoyant density and isoelectric point. They consisted of protein (53%), lipid (36%) and carbohydrate (11%), and the alpha-helix content was estimated to be 32%, differing from the reported values for human plasma-derived HBsAg (hHBsAg). Immunodiffusion analysis showed that the antigenic specificity of yHBsAg was identical to that of hHBsAg. Immunization of mice demonstrated that the immunogenicity of the yHBsAg was significantly higher than that of hHBsAg. </p>
キーワード hepatitis B surface antigen yeast Pre S2 immunogenicity recombinant yeast
Amo Type Article
発行日 1991-02
出版物タイトル Acta Medica Okayama
出版者 Okayama University Medical School
開始ページ 11
終了ページ 19
ISSN 0386-300X
NCID AA00508441
資料タイプ 学術雑誌論文
言語 English
論文のバージョン publisher
査読 有り
PubMed ID 1712147
Web of Sience KeyUT A1991FA75000002