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

2.50
Hdl Handle:
http://hdl.handle.net/10033/134620
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, Hui-Ling; Lünsdorf, Heinrich; Hecht, Hans-Jürgen; Tsai, Hsin
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.
Affiliation:
Development Center for Biotechnology, Taipei County 221, Taiwan, ROC.
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
Journal:
Micron (Oxford, England : 1993)
Issue Date:
Aug-2010
URI:
http://hdl.handle.net/10033/134620
DOI:
10.1016/j.micron.2010.01.005
PubMed ID:
20427191
Type:
Article
Language:
en
ISSN:
1878-4291
Appears in Collections:
publications of the research group vaccinology and applied microbiology (VAC)

Full metadata record

DC FieldValue Language
dc.contributor.authorChen, Hui-Lingen
dc.contributor.authorLünsdorf, Heinrichen
dc.contributor.authorHecht, Hans-Jürgenen
dc.contributor.authorTsai, Hsinen
dc.date.accessioned2011-06-27T14:21:00Z-
dc.date.available2011-06-27T14:21:00Z-
dc.date.issued2010-08-
dc.identifier.citationPorcine 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 Micronen
dc.identifier.issn1878-4291-
dc.identifier.pmid20427191-
dc.identifier.doi10.1016/j.micron.2010.01.005-
dc.identifier.urihttp://hdl.handle.net/10033/134620-
dc.description.abstractThe 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.en
dc.language.isoenen
dc.subject.meshAmino Acid Sequenceen
dc.subject.meshAnimalsen
dc.subject.meshChromatography, Affinityen
dc.subject.meshChromatography, Agaroseen
dc.subject.meshChromatography, Ion Exchangeen
dc.subject.meshElectrophoresis, Polyacrylamide Gelen
dc.subject.meshImage Processing, Computer-Assisteden
dc.subject.meshKineticsen
dc.subject.meshLungen
dc.subject.meshMicroscopy, Electronen
dc.subject.meshModels, Molecularen
dc.subject.meshMolecular Sequence Dataen
dc.subject.meshMolecular Weighten
dc.subject.meshOligopeptidesen
dc.subject.meshPeptidyl-Dipeptidase Aen
dc.subject.meshProtein Structure, Tertiaryen
dc.subject.meshSequence Analysis, Proteinen
dc.subject.meshSwineen
dc.titlePorcine pulmonary angiotensin I-converting enzyme--biochemical characterization and spatial arrangement of the N- and C-domains by three-dimensional electron microscopic reconstruction.en
dc.typeArticleen
dc.contributor.departmentDevelopment Center for Biotechnology, Taipei County 221, Taiwan, ROC.en
dc.identifier.journalMicron (Oxford, England : 1993)en

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