Pulmonary surfactant protein A isolation as a by-product of porcine pulmonary surfactant production
Biotechnology and Applied Biochemistry
; 40(2): 173-179, 2004.
Artigo
em Inglês
| Sec. Est. Saúde SP, SESSP-IBPROD, Sec. Est. Saúde SP, SESSP-IBACERVO
| ID: biblio-1060898
Biblioteca responsável:
BR78.1
Localização: BR78.1
ABSTRACT
A pulmonary surfactant reduces surface tension at the air/liquid interface of the alveoli and stabilizes alveoli at low lung volumes. Surfactant deficiency and dysfunction were shown to be present in a number of pulmonary diseases, and surfactant replacement therapy is the common clinical conduct. The hydrophilic SP-A (surfactant protein A) is absent when solvent extraction was used during exogenous surfactant production. Addition of SP-A to the surfactant preparation increases the surface activity and completely counteracts inhibition by blood proteins. SP-A recognizes and binds to carbohydrate structures on the surfaces of pathogenic micro-organisms, and acts as opsonins or cross-linking molecules by binding to a variety of cells that participate in the pulmonary immune response. The purification procedure yielded 206 mg of high-purity SP-A/kg of porcine lung, as judged by gel filtration, SDS/PAGE and Western blotting. The electrophoretic profiles obtained showed that pure SP-A consists of proteins of wide molecular mass in the range 26-36 kDa and a dimer in the range 56-60 kDa. The Western-blot results displayed the same band pattern profile after incubating the membrane using a commercially available polyclonal anti-SP-A antibody produced in goat. Gel-filtration experiments confirmed the molecular mass of SP-A in 10 mM NaCl solution. The isolated SP-A showed mannose-binding ability, representative of its functionality.
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Coleções:
Bases de dados nacionais
/
Brasil
Base de dados:
Sec. Est. Saúde SP
/
SESSP-IBACERVO
/
SESSP-IBPROD
Assunto principal:
Surfactantes Pulmonares
/
Proteína A Associada a Surfactante Pulmonar
Limite:
Animais
Idioma:
Inglês
Revista:
Biotechnology and Applied Biochemistry
Ano de publicação:
2004
Tipo de documento:
Artigo
Instituição/País de afiliação:
Instituto Butantan/BR