Purification of hog lung angiotensin Ⅰ-converting enzyme by affinity chromatography = Affinity chromatography 에 의한 돼지허파내 angiotensin Ⅰ전환효소의 정제

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.
Advisors
Lee, Hyun-Jae이현재
Publisher
한국과학기술원
Issue Date
1984
Identifier
64040/325007 / 000821007
Language
eng
Description

학위논문(석사) - 한국과학기술원 : 생물공학과, 1984.2, [ vi, 57 p. ]

Keywords

단백질 분리.

URI
http://hdl.handle.net/10203/28160
Link
http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=64040&flag=t
Appears in Collection
BS-Theses_Master(석사논문)
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