Conformation of group "a" epitope in hepatitis B surface antigen

Mun Ho Chun, Won Bong Park, Jin Woo Bok, Ha Won Kim, Eung Chil Choi, Byong Kak Kim

Research output: Contribution to journalArticle

Abstract

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 virtually 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-pg30.

Original languageEnglish (US)
Pages (from-to)347-355
Number of pages9
JournalArchives of Pharmacal Research
Volume15
Issue number4
DOIs
StatePublished - Dec 1 1992
Externally publishedYes

Fingerprint

Hepatitis B Surface Antigens
Conformations
Epitopes
Durapatite
Sepharose
Monoclonal Antibodies
Hepatitis B Antigens
Column chromatography
Ultracentrifugation
Ammonium Sulfate
Disulfides
Chromatography
Anti-Idiotypic Antibodies
Glycoproteins
Blood
Antigens
Antibodies
Proteins

Keywords

  • anti-idiotype antibody
  • competitive ELISA inhibition
  • epitope
  • HBsAg
  • idiotype antibody

ASJC Scopus subject areas

  • Molecular Medicine
  • Drug Discovery
  • Organic Chemistry

Cite this

Conformation of group "a" epitope in hepatitis B surface antigen. / Chun, Mun Ho; Park, Won Bong; Bok, Jin Woo; Kim, Ha Won; Choi, Eung Chil; Kim, Byong Kak.

In: Archives of Pharmacal Research, Vol. 15, No. 4, 01.12.1992, p. 347-355.

Research output: Contribution to journalArticle

Chun, Mun Ho ; Park, Won Bong ; Bok, Jin Woo ; Kim, Ha Won ; Choi, Eung Chil ; Kim, Byong Kak. / Conformation of group "a" epitope in hepatitis B surface antigen. In: Archives of Pharmacal Research. 1992 ; Vol. 15, No. 4. pp. 347-355.
@article{5c54b9ee00af4d6f9070652776fce305,
title = "Conformation of group {"}a{"} epitope in hepatitis B surface antigen",
abstract = "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 virtually 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-pg30.",
keywords = "anti-idiotype antibody, competitive ELISA inhibition, epitope, HBsAg, idiotype antibody",
author = "Chun, {Mun Ho} and Park, {Won Bong} and Bok, {Jin Woo} and Kim, {Ha Won} and Choi, {Eung Chil} and Kim, {Byong Kak}",
year = "1992",
month = "12",
day = "1",
doi = "10.1007/BF02974111",
language = "English (US)",
volume = "15",
pages = "347--355",
journal = "Archives of Pharmacal Research",
issn = "0253-6269",
publisher = "Pharmaceutical Society of Korea",
number = "4",

}

TY - JOUR

T1 - Conformation of group "a" epitope in hepatitis B surface antigen

AU - Chun, Mun Ho

AU - Park, Won Bong

AU - Bok, Jin Woo

AU - Kim, Ha Won

AU - Choi, Eung Chil

AU - Kim, Byong Kak

PY - 1992/12/1

Y1 - 1992/12/1

N2 - 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 virtually 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-pg30.

AB - 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 virtually 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-pg30.

KW - anti-idiotype antibody

KW - competitive ELISA inhibition

KW - epitope

KW - HBsAg

KW - idiotype antibody

UR - http://www.scopus.com/inward/record.url?scp=77951516816&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77951516816&partnerID=8YFLogxK

U2 - 10.1007/BF02974111

DO - 10.1007/BF02974111

M3 - Article

VL - 15

SP - 347

EP - 355

JO - Archives of Pharmacal Research

JF - Archives of Pharmacal Research

SN - 0253-6269

IS - 4

ER -