Porcine pulmonary angiotensin I-converting enzyme-Biochemical characterization and spatial arrangement of the N- and C-domains by three-dimensional electron microscopic reconstruction

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题名:	Porcine pulmonary angiotensin I-converting enzyme-Biochemical characterization and spatial arrangement of the N- and C-domains by three-dimensional electron microscopic reconstruction
作者:	Chen, HL (Chen, Hui-Ling) Lunsdorf, H (Luensdorf, Heinrich) Hecht, HJ (Hecht, Hans-Juergen) Tsai, H (Tsai, Hsin)
贡献者:	生科所
关键词:	Somatic angiotensin I-converting enzyme Pig lung N-domain C-domain Electron microscopy 3D reconstruction
日期:	2010-08
上传时间:	2011-12-09 14:08:29 (UTC+8)
摘要:	The somatic angiotensin I-converting enzyme (sACE; peptidyl-dipeptidase A; EC 3.4.15.1) was isolated from pig lung and purified to homogeneity. The purified enzyme has a molecular mass of about 180 kDa. Upon proteolytic cleavage, two approximately 90 kDa fragments were obtained and identified by amino-terminal sequence analysis as the N- and C-domains of sACE. Both purified domains were shown to be catalytically active. A 2.3 nm resolution model of sACE was obtained by three-dimensional electron microscopic reconstruction of negatively stained sACE particles, based on atomic X-ray data fitting. Our model shows for the first time the relative orientation of the sACE catalytically active domains and their spatial distance. (C) 2010 Elsevier Ltd. All rights reserved.
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