• Title/Summary/Keyword: IMAC

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의료 영상 관리와 통신 시스템

  • 문성기;안승옥
    • 전기의세계
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    • v.38 no.8
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    • pp.41-52
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    • 1989
  • 본 논문에서는 의료 IMACS와 관련된 새로운 디지탈 입력 장치들, 데이타베이스 시스템과 저장매체, 여러 종류의 Workstation, 통신 시스템등 기술적인 면을 많이 다루려 한다. 그리고 영상의 질과 자료의 양, 망의, 성능 분석, 영상화 시스템들과 방사선 정보 시스템과 다른 주변 기기들과의 접속에 따른 IMACS의 효과를 논하려 한다. 또한 지난 87년부터 Gorgetown University Hospital(GUH)은 미육군 의무단의 6,5백만불의 지원으로 가장 광범위한 의료 IMACS설비를 AT & T사와 공동 연구하고 설치하여, IMACS의 기술적 평가를 계속하여 왔다. 이와같이 실행되어 있는 경험을 통하여, 의료 IMACS의 임상 운영 효과와 더 나아가서 새로운 효과들을 검토함으로써 앞으로 보강되어져야 할 점들을 연구하려 한다.

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An Effective Method of Isolating Immunoglobulins from Bovine Plasma Proteins (도축혈액으로부터 면역단백질의 효과적인 분리법)

  • Choi, In-Wook;Lee, Hyun-Jung
    • Korean Journal of Food Science and Technology
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    • v.29 no.5
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    • pp.1067-1070
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    • 1997
  • Imunoglobulins from bovine plasma proteins were isolated by IMAC which $Cu^{2+}$ was chelated on a chelating sepharose fast flow gel. Most plasma proteins were eluted by 1st (0.01 M $Na_2HPO_4$, 0.5 M NaCl, pH 4.0) and 2nd elution buffers (0.01 M imidazol). According to the reverse phase HPLC analysis, it was found that proteins which were eluted by 1st elution buffer were mainly composed of serum albumin, while most IgG and transferrin were eluted by 2nd elution buffer. When protein fractions obtained by 2nd elution buffer was applied to ultra filtration system (molecular weight cut off: 100 kD), IgG was further purified. These results indicate that IMAC is an excellent tool for isolating imunoglobulins from plasma proteins.

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Development of Decision Tree Software and Protein Profiling using Surface Enhanced laser Desorption/lonization - Time of Flight - Mass Spectrometry (SELDI-TOF-MS) in Papillary Thyroid Cancer (의사결정트리 프로그램 개발 및 갑상선유두암에서 질량분석법을 이용한 단백질 패턴 분석)

  • Yoon, Joon-Kee;Lee, Jun;An, Young-Sil;Park, Bok-Nam;Yoon, Seok-Nam
    • Nuclear Medicine and Molecular Imaging
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    • v.41 no.4
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    • pp.299-308
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    • 2007
  • Purpose: The aim of this study was to develop a bioinformatics software and to test it in serum samples of papillary thyroid cancer using mass spectrometry (SELDI-TOF-MS). Materials and Methods: Development of 'Protein analysis' software performing decision tree analysis was done by customizing C4.5. Sixty-one serum samples from 27 papillary thyroid cancer, 17 autoimmune thyroiditis, 17 controls were applied to 2 types of protein chips, CM10 (weak cation exchange) and IMAC3 (metal binding - Cu). Mass spectrometry was performed to reveal the protein expression profiles. Decision trees were generated using 'Protein analysis' software, and automatically detected biomarker candidates. Validation analysis was performed for CM10 chip by random sampling. Results: Decision tree software, which can perform training and validation from profiling data, was developed. For CM10 and IMAC3 chips, 23 of 113 and 8 of 41 protein peaks were significantly different among 3 groups (p<0.05), respectively. Decision tree correctly classified 3 groups with an error rate of 3.3% for CM10 and 2.0% for IMAC3, and 4 and 7 biomarker candidates were detected respectively. In 2 group comparisons, all cancer samples were correctly discriminated from non-cancer samples (error rate = 0%) for CM10 by single node and for IMAC3 by multiple nodes. Validation results from 5 test sets revealed SELDI-TOF-MS and decision tree correctly differentiated cancers from non-cancers (54/55, 98%), while predictability was moderate in 3 group classification (36/55, 65%). Conclusion: Our in-house software was able to successfully build decision trees and detect biomarker candidates, therefore it could be useful for biomarker discovery and clinical follow up of papillary thyroid cancer.

Recombinant Expression and Purification of Functional XorII, a Restriction Endonuclease from Xanthomonas oryzae pv. oryzae

  • Hwang, Dong-Kyu;Cho, Jae-Yong;Chae, Young-Kee
    • Journal of Microbiology
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    • v.45 no.2
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    • pp.175-178
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    • 2007
  • An endonuclease from Xanthomonas oryzae pathovar oryzae KACC 10331, XorII, was recombinantly produced in Escherichia coli using a T7 system. XorII was purified using a combination of ion exchange and immobilized metal affinity chromatography (IMAC). An optimized washing protocol was carried out on an IMAC in order to obtain a high purity product. The final amount of purified XorII was approximately 2.5 mg/L of LB medium. The purified recombinant XorII was functional and showed the same cleavage pattern as PvuI. The enzyme activity tested the highest at $25^{\circ}C$ in 50 mM NaCl, 10 mM Tris-HCl, 10 mM $MgCl_{2}$, and 1 mM dithiothreitol at a pH of 7.9.

Retrospective analyses of the bottleneck in purification of eukaryotic proteins from Escherichia coli as affected by molecular weight, cysteine content and isoelectric point

  • Jeon, Won-Bae
    • BMB Reports
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    • v.43 no.5
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    • pp.319-324
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    • 2010
  • Experimental bioinformatics data obtained from an E. coli cell-based eukaryotic protein purification experiment were analyzed in order to identify any bottleneck as well as the factors affecting the target purification. All targets were expressed as His-tagged maltose-binding protein (MBP) fusion constructs and were initially purified by immobilized metal affinity chromatography (IMAC). The targets were subsequently separated from the His-tagged MBP through TEV protease cleavage followed by a second IMAC isolation. Of the 743 total purification trials, 342 yielded more than 3 mg of target proteins for structural studies. The major reason for failure of target purification was poor TEV proteolysis. The overall success rate for target purification decreased linearly as cysteine content or isoelectric point (pI) of the target increased. This pattern of pI versus overall success rate strongly suggests that pI should be incorporated into target scoring criteria with a threshold value.

Effects of pH on Purification of GFPuv/Cytochrome c-552 Fusion Protein

  • Lee, Sang-On;Hong, Eul-Jae;Choe, Jeong-U;Hong, Eok-Gi
    • 한국생물공학회:학술대회논문집
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    • 2003.04a
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    • pp.539-542
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    • 2003
  • Fusion gene of GFPuv and Cytochrome c-552 was inserted into the pTrcHis B vector and transferred to E. coli. A fusion protein of GFPuv and Cytochrome c-552 was expressed in BL21. This fusion protein was composed of a His-tag for purification using an immobilized metal affinity chromatography(IMAC). IMAC constitutes a rather facile means of unravelling the principles of recognition and, in particular, of identifying the counterligands on the protein surface, which interact with the ligated and immobilized metal ions. Histidine when present on the surface of a protein molecule under a favorable solvent condition, may serve as electron donors in coordination with the immobilized chelates of some transition metal ions$(Ni^{2+})$.

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