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

Chen, Hui-Ling; Lünsdorf, Heinrich; Hecht, Hans-Jürgen; Tsai, Hsin

dc.contributor.author	Chen, Hui-Ling
dc.contributor.author	Lünsdorf, Heinrich
dc.contributor.author	Hecht, Hans-Jürgen
dc.contributor.author	Tsai, Hsin
dc.date.accessioned	2011-06-27T14:21:00Z
dc.date.available	2011-06-27T14:21:00Z
dc.date.issued	2010-08
dc.identifier.citation	Porcine pulmonary angiotensin I-converting enzyme--biochemical characterization and spatial arrangement of the N- and C-domains by three-dimensional electron microscopic reconstruction. 2010, 41 (6):674-85 Micron	en
dc.identifier.issn	1878-4291
dc.identifier.pmid	20427191
dc.identifier.doi	10.1016/j.micron.2010.01.005
dc.identifier.uri	http://hdl.handle.net/10033/134620
dc.description.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.
dc.language.iso	en	en
dc.subject.mesh	Amino Acid Sequence	en
dc.subject.mesh	Animals	en
dc.subject.mesh	Chromatography, Affinity	en
dc.subject.mesh	Chromatography, Agarose	en
dc.subject.mesh	Chromatography, Ion Exchange	en
dc.subject.mesh	Electrophoresis, Polyacrylamide Gel	en
dc.subject.mesh	Image Processing, Computer-Assisted	en
dc.subject.mesh	Kinetics	en
dc.subject.mesh	Lung	en
dc.subject.mesh	Microscopy, Electron	en
dc.subject.mesh	Models, Molecular	en
dc.subject.mesh	Molecular Sequence Data	en
dc.subject.mesh	Molecular Weight	en
dc.subject.mesh	Oligopeptides	en
dc.subject.mesh	Peptidyl-Dipeptidase A	en
dc.subject.mesh	Protein Structure, Tertiary	en
dc.subject.mesh	Sequence Analysis, Protein	en
dc.subject.mesh	Swine	en
dc.title	Porcine pulmonary angiotensin I-converting enzyme--biochemical characterization and spatial arrangement of the N- and C-domains by three-dimensional electron microscopic reconstruction.	en
dc.type	Article	en
dc.contributor.department	Development Center for Biotechnology, Taipei County 221, Taiwan, ROC.	en
dc.identifier.journal	Micron (Oxford, England : 1993)	en
refterms.dateFOA	2018-06-12T22:50:42Z
html.description.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.