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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)
BMP-2-Enhanced Chondrogenesis Involves p38 MAPK-mediated Down-Regulation of Wnt-7a Pathway
진은정,강신성,이선영,최영애,정재창,Ok-Sun Bang 한국분자세포생물학회 2006 Molecules and cells Vol.22 No.3
The bone morphogenetic protein (BMP) family has been implicated in control of cartilage development. Here, we demonstrate that BMP-2 promotes chondrogenesis by activating p38 mitogen-activated protein kinase (MAPK), which in turn downregulates Wnt7a/β-catenin signaling responsible for proteasomal degradation of Sox9. Exposure of mesenchymal cells to BMP-2 resulted in upregulation of Sox9 protein and a concomitant decrease in the level of β-catenin protein and Wnt-7a signaling. In agreement with this, the interaction of Sox9 with β-catenin was inhibited in the presence of BMP-2. Inhibition of the p38 MAPK pathway using a dominant negative mutant led to sustained Wnt-7a signaling and decreased Sox9 expression, with consequent inhibition of precartilage condensation and chondrogenic differentiation. Moreover, overexpression of β-catenin caused degradation of Sox9 via the ubiquitin/26S proteasome pathway. Our results collectively indicate that the increase in Sox9 protein resulting from downregulation of β-catenin/Wnt-7a signaling is mediated by p38 MAPK during BMP-2 induced chondrogenesis in chick wing bud mesenchymal cells.
사람 α - Proteinase Inhibitor 의 분리 및 분석
방옥선,최윤정,강신성 ( Ok Sun Bang,Yoon Jeong Choi,Shin Sung Kang ) 생화학분자생물학회 1988 BMB Reports Vol.21 No.4
For the preliminary step to make and characterize the monoclonal antibodies against human alpha-1-proteinase inhibitor (α₁-PI), the α₁-PI molecules were isolated from 500 ml of normal human serum through the procedures including salt precipitation, Cibacron blue F3GA-agarose, DEAE-cellulose, concanavalin A-Sepharose and Sephadex G-100 gel chromatography. The isolated α₁-PI proparation showed a single band both on polyacrylamide gel electrophoresis and SDS-polyacrylamide gel electrophoresis and also a single precipitin arc against anti-normal human serum and anti-human α₁-PI antiserum on immunoelectrophoresis. The recovery of α₁-PI was 52.42 ㎎ total and the specific activity of this protein was 14.29 unit/㎎ of protein. The CNB-cleaved peptide fragments (Fr I : 64-220; Fr II : 243-351; Fr III : 1-63) were also isolated to homogeneity.
사람 ${\alpha}_1$-Proteinase Inhibitor 의 분리 및 분석
방옥선,최윤정,강신성,Bang, Ok-Sun,Choi, Yoon-Jeong,Kang, Shin-Sung 생화학분자생물학회 1988 한국생화학회지 Vol.21 No.4
사람의 ${\alpha}_1$-proteinase inhibitor (${\alpha}_1-PI$)에 대한 단일클론 항체의 생산 및 분석을 위하여 사람의 혈장을 재료로 추출법, Cibacron blue F3GA-agarose, DEAE-cellulose, Concanavalin A-Sepharose 4B, Sephadex G-100 등의 크로마토그라피 방법으로 ${\alpha}_1-PI$를 분리하였다. 분리 한 ${\alpha}_1-PI$는 alkaline polyacrylamide gel electrophoresis 및 SDS-PAGE 에서 단일 밴드로 나타났고, 또 immunoelectrophoresis에서도 anti-human serum 및 anti-${\alpha}_1-PI$에 대해 단일 침전 arc를 나타내어 순수분리되었음을 확인하였다. 정상인 혈장 500 ml로부터 분리된 ${\alpha}_1-PI$의 회수율은 약 37 %로서 52.41 mg이었고, 트립신 저해능의 비활성도는 14.29 unit/mg protein이었다. 이와같이 하여 순수정제된 ${\alpha}_1-PI$를 CNBr로 처리하여 3 가지의 $CNBr^-$ 펩티드 분획인 FrI (아미노산 잔기 64-220), Fr II (아미노산 잔기 243-351) 및 Fr III (아미노산 잔기 1-63)을 각각 분리하였다. For the preliminary step to make and characterize the monoclonal antibodies against human alpha-I-proteinase inhibitor (${\alpha}_1-PI$), the ${\alpha}_1-PI$molecules were isolated from 500 ml of normal human serum through the procedures including salt precipitation, Cibacron blue F3GA-agarose, DEAE-cellulose, concanavalin A-Sepharose and Sephadex G-100 gel chromatography. The isolated ${\alpha}_1-PI$ proparation showed a single band both on polyacrylamide gel electrophoresis and SDS-polyacrylamide gel electrophoresis and also a single precipitin arc against anti-normal human serum and anti-human ${\alpha}_1-PI$) antiserum on immunoelectrophoresis. The recovery of $a_1$-PI was 52.42 mg total and the specific activity of this protein was 14.29 unit/mg of protein. The CNB-c1eaved peptide fragments (Fr I: 64-220: Fr II: 243-351; Fr III: 1-63) were also isolated to homogeneity.
단핵구 분화에 있어서 fibronectin 수용체의 역할
강신성,방옥선,강희갑,이영섭,박의균 경북대학교 유전공학연구소 1995 遺傳工學硏究所報 Vol.10 No.1
The interaction between flbronectin (FN) and its receptor controls cell attachment and migration, two crucial events during monocyte development and differentiation. To investigate the functional role of FN and its receptor, we have studied adhesion of monocyte to two different regions of FN (38- and 85-kDa domain), as well as the expression of the integrin during monocyte differentiation. Anti-integrin β1 subunit antibody completely blocked the attachment of FN-coated latex beads to macrophage, but the effect of anti-integrin α4 antibody was much less significant. Rat monocyte expressed integrin α4β1 predominantly, while macrophage pressed a5f31 as analyzed by flow cytometer and western blot. From these results, it can be suggested that these two integrins play different role: during monocyte differentiation.
단핵구 분화에 대한 Fibronection 및 그 단편의 역할
강신성,방옥선,이영섭 경북대학교 유전공학연구소 1995 遺傳工學硏究所報 Vol.10 No.1
Monocyte interaction with fibronectin (FN) mediates specific cell surface receptors and results in cell attachment and differentiation. Several cell-mediated activities for various fragments of FN have been documented. To investigate the regulatory mechanisms of monocyte differentiation by cell binding domains of FN and their receptors, cell attachment-, cell migration-, and its respective inhibition assay were carried out. Monocyte recognizes 38-kDa domain distinctively from its recognition of 85-kDa domain, and the heparin-binding site of the 38-kDa fragment is not involved in monocyte adhesion. Based on these experimental results, it can be suggested that monocyte/macrophage interacts with at least two different sites in FN, which is critical step in cell adhesion and (or) migration.
태반형 알칼라인 포스파타아제 유전형에 대한 단일클론 항체
강신성,강희갑,윤종희,방옥순,이영섭 한국유전학회 1993 Genes & Genomics Vol.15 No.4
A total of nine monoclonal antibodies (MAbs) against common phonotypes of human placental alkaline phosphatase (PLAP) was produced by hybridoma using a mixture of PLAP subtypes (type 1+2+3) as antigen. Six of these reacted only with PLAP, but not with intestinal and liver alkaline phosphatases. Three out of these six MAbs have been found to discriminate at least one of the product of three common alleles from others, while the other three MAbs reacted with the six common allelic varients. The results suggest that anti-PLAP MAbs can be used as probes to discriminate among allelic varients of PLAP.