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항AK3 단클론 항체의 single chain fragment variable(ScFv) 제작 및 생화학적 특성 연구
김백길,김효준 한양대학교 이학기술연구소 2002 이학기술연구지 Vol.5 No.-
단클론 항체는 항원에 대한 높은 특이성을 갖는다. 이러한 특성은 혈액이나 조직에 존재하는 특정 항원을 검출하기 위해 널리 이용되고 있다. 그러나 혈액 내에 존재하는 human anti mouse antibody (HAMA)와 같은 plasma protein 에 의한 단클론 항체와의 결합에 의해 특이성이 심하게 저하되는 현상이 나타난다. 최근 Fc 부분이 제거된 단클론 항체가 혈액내 비특이적 결합을 줄일 수있음이 ㅂ조고되고 있으며, 이러한 목적으로 phage display system을 이용한 항체공학이 Fc부분을 제거하기 위해 방법론적으로 활용되고 있다. 본 연구에서는 phage display system을 이용하여, 항 adenylate kinase isoenzyme 3(AK3) 단클론 항체 SJA3-86으로부터 single chain fragment variable gene(ScFv)을 cloning하였고, E.coli expression system을 통해 재조합 항체 ScF86을 발현시켰다. ScF86의 cDNA 염기배열로부터 유추한 CDR1, 2 및 3는 negative charge의 amino acid가 다수 포함되어 염기성 효소인 AK3를 전기적으로 효율적인 인식이 이루어짐을 확인하였고, parental antibody인 SJA3-86이 conformational epitope보다 denatured epitope을 효과적으로 인식하는 항원-항제 반응서으을 유지하고 있었다. 그러나 Fc 부분이 절단되고, 아미노산10개로 구성된 linker peptide가 도입된 결과 항원에 대한 Kd값은 1.1×10-9으로 원래의 약60%의 친화력을 단백공학에 의한 형태변화에도 불구하고 항원의 인식능력은 크게 변하지 않았다. 이러한 결과로 ScF86은 혈액내 비특이적 결합을 제거한 항체공학적 단클론 항체로서 임상적으로 유용하게 활용될 수 있을 것으로 사료된다. Abstract : As monoclonal antibody has high specificity for a antigen, it is widely used for the detection of spexific antigen in blood or tissues. however, non-specific binding of monoclonal antibody in blood is still troublesome. Recently, it is reported that antibody without Fc reactivity can decrease non-specific binding in blood. To remove Fc reactivity antibody engineering technique using phage display system has been used developed. By utilizing phage display system we constructed ScFv(Single chain Fragment variable)fragment of monoclonal antibody against human adenylate kinase isozymes 3(AK3) expressed as a single peptide in E.coli. From the analysis of amino acids seuuence we verified that the CDRs of ScF86 contained many negatively charged amino acids, which were reasonable to interact with AK3 by charge interaction. However the deletion of Fc region and addition of linker peptide caused the lower 1.I× 10-9 M of ScF86 which is the affinity decrease by that of 60% of parentalantibody. This deviation is very small one compaired with other general protein engineering on receptor-ligand reactivities and the lowered affinity is not socntical in the further usage of the antibody. The refgre, we successfully constructed there combinant antibody ScF86 against AK3 that eliminate the Plasma-derivated non-specific bindings in immunochemical studies.
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Lymphangiogenesis in Breast Cancer Correlates with Matrix Stiffness on Shear-Wave Elastography
조남훈,차윤진,육지현,김백길,정우희 연세대학교의과대학 2016 Yonsei medical journal Vol.57 No.3
Purpose: To correlate tumor stiffness and lymphangiogenesis in breast cancer and to find its clinical implications. Materials and Methods: A total of 140 breast cancer patients were evaluated. Tumor stiffness was quantitatively measured by shear-wave elastography in preoperative ultrasound examination, calculated as mean elasticity value (kPa). Slides of resected breast cancer specimens were reviewed for most fibrotic area associated with tumor. D2-40 immunohistochemical staining was applied for fibrotic areas to detect the lymphatic spaces. Microlymphatic density, tumor stiffness, and clinicopathologic data were analyzed. Results: Higher elasticity value was associated with invasive size of tumor, microlymphatic density, histologic grade 3, absence of extensive intraductal component, presence of axillary lymph node metastasis, and Ki-67 labeling index (LI) in univariate regressionanalysis, and associated with Ki-67 LI and axillary lymph node metastasis in multivariate regression analysis. Microlymphaticdensity was associated histologic grade 3, mean elasticity value, and Ki-67 LI in univariate regression analysis. In multivariate regression analysis, microlymphatic density was correlated with mean elasticity value. Conclusion: In breast cancer, tumor stiffness correlates with lymphangiogenesis and poor prognostic factors.
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Ovarian Clear Cell Carcinoma Sub-Typing by ARID1A Expression
최재윤,조남훈,한현호,김영태,이주현,김백길,강수기 연세대학교의과대학 2017 Yonsei medical journal Vol.58 No.1
Purpose: Loss of AT-rich DNA-interacting domain 1A (ARID1A) has been identified as a driving mutation of ovarian clear cell carcinoma (O-CCC), a triple-negative ovarian cancer that is intermediary between serous and endometrioid subtypes, in regards to molecular and clinical behaviors. However, about half of O-CCCs still express BAF250a, the protein encoded by ARID1A. Herein,we aimed to identify signatures of ARID1A-positive O-CCC in comparison with its ARID1A-negative counterpart. Materials and Methods: Seventy cases of O-CCC were included in this study. Histologic grades and patterns of primary tumor, molecular marker immunohistochemistry profiles, and clinical outcomes were analyzed. Results: Forty-eight (69%) O-CCCs did not express BAF250a, which were designated as “ARID1A-negative.” The other 22 (31%) O-CCCs were designated as “ARID1A-positive.” ARID1A-positive tumors were more likely to be histologically of high grades (41% vs. 10%, p=0.003), ERβ-positive (45% vs. 17%, p=0.011), and less likely to be HNF1β-positive (77% vs. 96%, p=0.016) and E-cadherin-positive (59% vs. 83%, p=0.028) than ARID1A-negative tumors. Patient age, parity, tumor stage were not significantly different in between the two groups. Cancer-specific survival was not significantly different either. Conclusion: We classified O-CCCs according to ARID1A expression status. ARID1A-positive O-CCCs exhibited distinct immunohistochemicalfeatures from ARID1A-negative tumors, suggesting a different underlying molecular event during carcinogenesis.
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