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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Title:	Porcine pulmonary angiotensin I-converting enzyme-Biochemical characterization and spatial arrangement of the N- and C-domains by three-dimensional electron microscopic reconstruction
Authors:	Chen, HL (Chen, Hui-Ling) Lunsdorf, H (Luensdorf, Heinrich) Hecht, HJ (Hecht, Hans-Juergen) Tsai, H (Tsai, Hsin)
Contributors:	生科所
Keywords:	Somatic angiotensin I-converting enzyme Pig lung N-domain C-domain Electron microscopy 3D reconstruction
Date:	2010-08
Issue Date:	2011-12-09 14:08:29 (UTC+8)
Abstract:	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.
Appears in Collections:	[Graduate Institute of Biotechnology ] journal articles

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