Porcine pulmonary angiotensin I-converting enzyme--biochemical characterization and spatial arrangement of the N- and C-domains by three-dimensional electron microscopic reconstruction.
Micron
; 41(6): 674-85, 2010 Aug.
Article
en En
| MEDLINE
| ID: mdl-20427191
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.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Porcinos
/
Peptidil-Dipeptidasa A
/
Pulmón
Límite:
Animals
Idioma:
En
Revista:
Micron
Asunto de la revista:
DIAGNOSTICO POR IMAGEM
Año:
2010
Tipo del documento:
Article