ID 32216
JaLCDOI
フルテキストURL
著者
Konobe, Takeo Osaka University
Ishikawa, Nobuyoshi Osaka University
Gohda, Hideo Osaka University
Fukai, Konosuke Osaka University
Okabe, Akinobu Kagawa Medical School
抄録

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.

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
45巻
1号
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
OAI-PMH Set
岡山大学
論文のバージョン
publisher
査読
有り
Submission Path
amo/vol45/iss1/2
PubMed ID
Web of Sience KeyUT
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