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강신성,방옥선,강희갑,손종경,Kang, Shin-Sung,Bang, Ok-Sun,Kang, Hee-Kap,Sonn, Jong-Kyung 생화학분자생물학회 1988 한국생화학회지 Vol.21 No.4
Alpha-1-proteinase inhibitor(${\alpha}_1-PI$)로 면역시킨 Balb/c 마우스 비장세포와 SP 2/0-Ag 14 마우스 미에로마 세포를 융합시키는 하이브리도마 기법으로 모노클론 항체 생산을 실시하였다. 하이브리드클론들이 생산하는 항체들과 ${\alpha}_1-PI$와의 반응성은 ELISA로 분석하였으며, 양성클론을 제한희석법으로 클로닝하여 7클론의 항-${\alpha}_1-PI$ 특이 클론세포를 얻었고, 이들의 단일클론성을 확인하였다. 7클론 중 5클론이 생산하는 모노클론항체는 항원에 대한 결합상수가 $0.1-1.1{\times}10^9M^{-1}$의 $IgG_1(k$) 이었고, 이들 항체의 항원 특이성을 ${\alpha}_1-PI$의 CNBr-peptide 분획을 이용한 Western blot를 실시한 결과 FrI(아미노산 잔기 64-220)에 특이한 것이 4클론, Fr II (243-351)에 특이한 것이 1클론이었고, 나머지 2클론의 특이성은 결정할 수 없었다. Monoclonal antibodies (MAbs) against human ${\alpha}_1-PI$ was produced by hybridizing SP 2/0-Ag 14 mouse myeloma cells with spleen cells of Balb/c mice immunized with ${\alpha}_1-PI$. The resulting hybridoma clones were screened for their ability to bind ${\alpha}_1-PI$ by ELISA. Seven positive stable monoclones were obtained by cloning three times in serial dilutions, and each antibody was identified to be homogeneous by several criterial By western bloting analysis using CNBr-cleavage peptide fragments (Fr I: amino acid residues 64-220; Fr II: 243-351; Fr III: 1-63), four of these monoclones were found to synthesize MAb specific to Fr I, and one clone to Fr II. But MAbs of the other two clones showed reactivity only to intact $a_1$-PI. Five of our monoclones were appeared to synthesize $IgG_1(k$) antibodies having affinity constant in the range $0.1-1.1{\times}10^9M^{-1}$.
하이브리도마 방법에 의한 항 α - Proteinase Inhibitor 모노클론항체의 생산과 분석
강신성,방옥선,강희갑,손종경 ( Shin Sung Kang,Ok Sun Bang,Hee Kap Kang,Jong Kyung Sonn ) 생화학분자생물학회 1988 BMB Reports Vol.21 No.4
Monoclonal antibodies (MAbs) against human α₁-PI was produced by hybridizing SP 2/0 -Ag 14 mouse myeloma cells with spleen cells of Balb/c mice immunized with a α₁-PI. The resulting hybridoma clones were screened for their ability to bind α₁-PI by ELISA. Seven positive stable monoclones were obtained by cloning three times in serial dilutions, and each antibody was identified to be homogeneous by several criterial. By western bloting analysis using CNBr-cleavage peptide fragments (Fr I: amino acid residues 64-220; Fr II: 243-351; Fr III : 1-63), four of these monoclones were found to synthesize MAb specific to Fr I, and one clone to Fr II. But MAbs of the other two clones showed reactivity only to intact α₁-PI. Five of our monoclones were appeared to synthesize IgG₁(k) antibodies having affinity constant in the range 0.1-1.1×10^9 M^(-1)