Interaction of pulmonary surfactant-associated protein (SP-A) with surfactant lipids.
Indian J Biochem Biophys
;
1992 Oct; 29(5): 433-7
Artigo
em Inglês
| IMSEAR
| ID: sea-27696
ABSTRACT
A pulmonary surfactant-associated protein complex with components of 36, 32 and 28 kDa was isolated from human lung homogenates and reassembled with surfactant lipids prepared as small unilamellar liposomes. The role of divalent cations in the assembly of this recombinant lipoprotein complex was studied by monitoring the changes in turbidity, intrinsic tryptophanyl fluorescence and surface activity. The protein-facilitated lipid aggregation was promoted on addition of 5 to 20 mM Ca2+. Intrinsic fluorescence measurements on SP-A (28-36 kDa) indicated that the tryptophan side chains were in a relatively hydrophobic environment, that the wavelength of maximum fluorescence emission and also the relative fluorescence, were changed upon the binding of lipid. Tryptophanyl fluorescence of the lipoprotein assembly was quenched as indicated by a reduction in the effective Stern-Volmer constant. These results suggest that Ca2+ lipid-protein interactions are involved in the structure and function of extracellular lung surfactant assembly.
Texto completo:
DisponíveL
Índice:
IMSEAR (Sudeste Asiático)
Assunto principal:
Proteolipídeos
/
Espectrometria de Fluorescência
/
Surfactantes Pulmonares
/
Humanos
/
Masculino
/
Cinética
/
Glicoproteínas
/
Adulto
/
Proteína A Associada a Surfactante Pulmonar
/
Proteínas Associadas a Surfactantes Pulmonares
Idioma:
Inglês
Revista:
Indian J Biochem Biophys
Ano de publicação:
1992
Tipo de documento:
Artigo
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