DC Field | Value | Language |
---|---|---|
dc.contributor.advisor | Lee, Hyun-Jae | - |
dc.contributor.advisor | 이현재 | - |
dc.contributor.author | Kang, Chang-Joong | - |
dc.contributor.author | 강창중 | - |
dc.date.accessioned | 2011-12-12T08:55:57Z | - |
dc.date.available | 2011-12-12T08:55:57Z | - |
dc.date.issued | 1984 | - |
dc.identifier.uri | http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=64040&flag=dissertation | - |
dc.identifier.uri | http://hdl.handle.net/10203/28160 | - |
dc.description | 학위논문(석사) - 한국과학기술원 : 생물공학과, 1984.2, [ vi, 57 p. ] | - |
dc.description.abstract | The purification of angiotensin I-converting enzyme which is known to act as a key enzyme in the control of blood pressure through the Renin-Angiotensin-Aldosterone system, was achieved using affinity chromatography as the principal purification step. The angiotensin I-converting enzyme was partially purified from hog lung homogenates by acidification, DEAE-cellulose chromatography and ultrafiltration. The kinetic properties and the effect of sodium chloride have showed the known characteristics of angiotensin I-converting enzyme. Therefore, it was confirmed that the enzyme was angiotensin I-converting anzyme. An effective affinity gel was prepared on Sepharose 6B matrix using succinylL-proline competitive inhibitor as a ligand and spacer arm was introduced by 1,6-hexanediamine between the matrix and a ligand. With this affinity column, the enzyme preparation showed high degree of purity and good purification yield. | eng |
dc.language | eng | - |
dc.publisher | 한국과학기술원 | - |
dc.subject | 단백질 분리. | - |
dc.title | Purification of hog lung angiotensin Ⅰ-converting enzyme by affinity chromatography | - |
dc.title.alternative | Affinity chromatography 에 의한 돼지허파내 angiotensin Ⅰ전환효소의 정제 | - |
dc.type | Thesis(Master) | - |
dc.identifier.CNRN | 64040/325007 | - |
dc.description.department | 한국과학기술원 : 생물공학과, | - |
dc.identifier.uid | 000821007 | - |
dc.contributor.localauthor | Lee, Hyun-Jae | - |
dc.contributor.localauthor | 이현재 | - |
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