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논문 기본 정보

자료유형
학술저널
저자정보
Chun, Mun-Ho (Department of Microbial Chemistry, College of Pharmacy, Seoul National University) Park, Won-Bong (Seoul Women's University) Bok, Jin-Woo (Department of Microbial Chemistry, College of Pharmacy, Seoul National University) Kim, Ha-Won (Department of Microbial Chemistry, College of Pharmacy, Seoul National University) Choi, Eung-Chil (Department of Microbial Chemistry, College of Pharmacy, Seoul National University) Kim, Byong-Kak (Department of Microbial Chemistry, College of Pharmacy, Seoul National University)
저널정보
대한약학회 Archives of pharmacal research : a publication of the Pharmaceutical Society of Korea Archives of pharmacal research : a publication of the Pharmaceutical Society of Korea 제15권 제4호
발행연도
1992.1
수록면
347 - 355 (9page)

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To elucidate structure of group "a" epitope, mouse antibodies that express idiotype monoclonal antibody and anti-idiotype monoclonal antibody against the group specific "a" determinant were purified by hydroxyapatite column. To obtain hepatitis B surface antigens (HBsAg). HBsAg positive blood was sequencially purified by ammonium sulfate precipitation, hydroxyapatite, sepharose 4B column chromatography and ultracentrifugation. The major protein (p25) and glycoprotein (gp30) of HBsAg were isolated by concanavalin-A-sepharose 4B. The ability of p25-gp30 among the HBsAg to inhibit the idiotype-anti-idiotype reaction was dependent on conformation, since reduced and alkylated p25-gp30 virtualy lost their inhibitory capacity when compared to native HBsAg. The data suggest that hepatitis B antigen is a conformational antigen critically dependent upon the disulfide bonds of p25-gp30.

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