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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.
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.
Comparison of Some Properties of Alkaline Phosphatase from Pekin Duck
Bang, Ok Sun,Kang, Shin-Sung 慶北大學校 自然科學大學 1985 自然科學論文集 Vol.3 No.-
집오리의 腎臟, 肝 및 腸粘膜 alkaline phosphatase(ALP)의 특성들을 比較 分析하여 다음과 같은 結果를 얻었다. Alkaline acrylamide gel 電氣泳動時 이동속도는 세 isozyme이 유사했으나, SDS-PAGE에서는 신장 효소가 간 및 장점낙효소보다 빨랐으므로, 세가지 효소는 유사한 化學的 構成을 하지만, 分子의 크기는 신장 ALP가 가장 큼을 알았다. p-Nitrophenyl phosphate를 기질로 하였을 때 간, 장점막 및 신장 ALP의 最適 pH는 各各 9.0, 9.0∼9.4 및 9.4∼10.0이었고, 熱安定性은 신장효소가 가장 낮았다. Mg^2+은 간, 신장, 장점막 ALP의 順으로 크게 효소활성을 증가시켰고, Ca^2+은 세 효소활성에 거의 影響을 주지 않았으며, Zn^2+은 신장효소에 대해 가장 沮害效果가 컸다. Phosphate이온은 세 효소에 대해 competitive 저해작용을 보였고, L-phenylalanine은 장점막 ALP에 대해 강력한 uncompetitive 阻害劑로 作用하였다.
돼지 血淸 alpha-1-protease inhibitor 의 分離
박성희,방옥선,강신성 경북대학교 1987 論文集 Vol.43 No.-
For the preliminary step to characterize the structural and immunological relationship of alpha-1-protease inhibitor molecule among mammalian species, alpha-1-protease inhibitor was purified from porcine serum through the procedures of salt fractionation, Cibacron blue F3GA-agarose, DEAE-cellulose, Concanavalin A-Sepharose and Sephadex G-100 gel chromatography. The specific inhibitory activity of purified porcine alpha-1-protease inhibitor against porcine trypsin was 9.59 unit/㎎ of protein, and the recovery was 26% with purification factor of 105-fold. The isolated alpha-1-protease inhibitor showed a single band on alkaline polyacrylamide gel electrophoresis and a single precipitin arc against rabbit anti-porcine serum on immunoelctrophoresis, which indicates that the alpha-1-protease inhibitor preparation is pure. This alpha-1-protease inhibitor also displayed a single band on SDS-polyacrylamide gel electrophoresis. The molecular weight of porcine alpha-1-protease inhibitor was estimated to be about 60,000 by SDS-polyacrylamide gel electrophoresis, and no immunological identity with human alpha-1-protease inhibitor was found.
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)
항-AFP 단클론항체를 이용한 암의 진단 및 치료효과의 검토
박대규,방옥선,강신성,조동택 경북대학교 유전공학연구소 1988 遺傳工學硏究所報 Vol.3 No.1
By noncompetitive ELISA using anti-AFP MAbs, it was confirmed that screening of serum AFP level is essential in diagnosis of the hepatocellular carcinoma. By indirect immunofluorescence technique, anti AFP MAbs were found to react with the surface of hepatoma cells (70%) and MCF-7 breastocarcinoma cells (45%), but not with ME-180 cervix carcinoma cells. The purified anti-AFP MAbs were coupled with RTA to form immunotoxin, whose effectiveness in in vitro killing of target cells was evaluated by cytotoxicity assay. The results showed that this immunotoxin was specifically cytotoxic to hepatocellular carcinoma cells.
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.
암-특이 항원인 alpha-Fetoprotein 에 대한 모노클론항체의 생산 및 분석
박대규,방옥선,강신성,조동택,송방호 경북대학교 유전공학연구소 1987 遺傳工學硏究所報 Vol.2 No.1
Monoclones secreting anti-human alpha-fetoprotein(AFP) were produced by hybridizing SP 2/0-Ag 14 mouse myeloma cells with spleen cells of Balb/c mice immunized with AFP. Two subclones (D-6 & E-6) were expanded as ascite tumors in syngenic mice, and immunoglobulins were purified from ascitic fluid. Each antibody was identified to be homogeneous monoclonal antibody (McAb) by several criteria, and the affinity constant of D-6 and E-6 McAb to AFP was calculated to be 4.2×10^(-8) and 6.4×10^(-8) M^(-1), respectively. With these McAbs sensitive and accurate enzyme linked immunosorbent assay method was established.