DC Field | Value | Language |
---|---|---|
dc.contributor.advisor | Rhee, Joon-Shick | - |
dc.contributor.advisor | 이준식 | - |
dc.contributor.author | Lee, Ho-Jae | - |
dc.contributor.author | 이호재 | - |
dc.date.accessioned | 2011-12-12T07:52:43Z | - |
dc.date.available | 2011-12-12T07:52:43Z | - |
dc.date.issued | 2000 | - |
dc.identifier.uri | http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=157748&flag=dissertation | - |
dc.identifier.uri | http://hdl.handle.net/10203/27476 | - |
dc.description | 학위논문(박사) - 한국과학기술원 : 생물과학과, 2000.2, [ xii, 180 p. ] | - |
dc.description.abstract | Matrix metalloproteinases (MMPs) have been implicated in a variety of disease states, including rheumatoid arthritis, periodontal disease, tumor invasion, and metastasis. In the MMP family, MMP-2 (gelatinase A) is unique in its ability to cleave type Ⅳ collagen, a principal structural components of basement membrane, and has been focused on as a pharmacological target. Consequently, specific inhibitors of MMP-2 may be of value in the therapy of cancers as well as other disease states involving tissue remodeling. ProMMP-2 was purified from a conditioned media of T98G human glioblastoma cells. Tissue inhibitor of metalloproteinase-2 (TIMP-2) complexed proMMP-2 and TIMP-2 free proMMP-2 were separated by heparin affinity HPLC. The proMMP-2 was homogeneous on SDS-PAGE, with a molecular weight of 64-kDa without reduction. In addition, TIMP-2 and proMMP-2 were separated from the TIMP-2 complexed proMMP-2 by reverse phase HPLC in the presence of trifluoroacetic acid. Two high-throughput screening assay methods were developed with the purified proMMP-2. As results, a fluorescence detection method using 96-well microplate was used as a primary screening system and a direct reaction injection method was used for the confirmation of inhibitory activities of screening samples. In the course of screening for MMP-2 inhibitors from fungi, a fungal strain F50733 was selected. The strain F50733 was identified as Westerdykella multispora on the basis of its cultural and morphological characteristics. The inhibitors of MMP-2, designated gelastatins A and B, and their precursor, dykellic acid were isolated from the culture broth of W. multispora F507343 by successive chromatographies and preparative HPLC. The structures of gelastatins A and B, and dykellic acid were determined by spectroscopic analysis of UV, IR, FAB-MS, $^1H-$, $^{13}C-NMR$, DEPT, HMQC, HMBC, and NOESY. Gelastatins A and B were determined to be 3-(5E-hexa-2E,4E-dienylidene-2-oxo-5,6-dihydro-2H-pyran-3-yl)-pr... | eng |
dc.language | eng | - |
dc.publisher | 한국과학기술원 | - |
dc.subject | Dykellic acid | - |
dc.subject | Gelastatin | - |
dc.subject | Inhibitor | - |
dc.subject | Matrix metalloproteinase | - |
dc.subject | Tumor invasion | - |
dc.subject | 암 침윤 | - |
dc.subject | 다이켈릭 산 | - |
dc.subject | 젤라스타틴 | - |
dc.subject | 저해제 | - |
dc.subject | 메트릭스 금속단백분해효소 | - |
dc.title | Characterization of new matrix metalloproteinases inhibitors from westerdykella multispora F50733 | - |
dc.title.alternative | Westerdykella multispora F50733 균주가 생산하는 새로운 메트릭스 금속단백분해효소 저해물질의 특성 | - |
dc.type | Thesis(Ph.D) | - |
dc.identifier.CNRN | 157748/325007 | - |
dc.description.department | 한국과학기술원 : 생물과학과, | - |
dc.identifier.uid | 000965329 | - |
dc.contributor.localauthor | Rhee, Joon-Shick | - |
dc.contributor.localauthor | 이준식 | - |
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