Lung surfactant protein SP-C from human, bovine, and canine sources contains palmityl cysteine thioester linkages.
Am J Physiol
; 261(2 Pt 1): L118-25, 1991 Aug.
Article
en En
| MEDLINE
| ID: mdl-1872406
ABSTRACT
Lung surfactant is a complex mixture of lipids and proteins that coats the alveoli to reduce surface tension and prevent airspace collapse. One of the principal protein constituents, surfactant protein C (SP-C), has been characterized following isolation from human, canine, and bovine sources. In each species, this highly hydrophobic protein is composed of 33-35 amino acids, the differences being due to NH2-terminal heterogeneity. A COOH-terminal leucine is conserved throughout. The cysteines in each species were found by fast atom bombardment mass spectrometry to be present as thioesters of palmitic acid. Acylation of recombinant SP-C with palmityl coenzyme A, followed by characterization before and after release of the acyl group with 1,4-dithiothreitol, provided corroborating evidence for the native structure.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Ácidos Palmíticos
/
Proteolípidos
/
Compuestos de Sulfhidrilo
/
Surfactantes Pulmonares
/
Cisteína
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Am J Physiol
Año:
1991
Tipo del documento:
Article