Passiflin, a novel dimeric antifungal protein from seeds of the passion fruit.
Phytomedicine
; 16(2-3): 172-80, 2009 Mar.
Article
em En
| MEDLINE
| ID: mdl-19200704
ABSTRACT
The intent was to isolate an antifungal protein from seeds of the passion fruit (Passiflora edulis) and to compare its characteristics with other antifungal proteins and bovine beta-lactoglobulin in view of its N-terminal amino acid sequence similarity to beta-lactoglobulin. The isolation procedure entailed ion-exchange chromatography on Q-Sepharose, hydrophobic interaction chromatography on Phenyl-Sepharose, ion-exchange chromatography on DEAE-cellulose, and FPLC-gel filtration on Superdex 75. The isolated 67-kDa protein, designated as passiflin, exhibited an N-terminal amino acid sequence closely resembling that of bovine beta-lactoglobulin. It is the first antifungal protein found to have a beta-lactoglobulin-like N-terminal sequence. Its dimeric nature is rarely found in antifungal proteins. It impeded mycelial growth in Rhizotonia solani with an IC(50) of 16 microM and potently inhibited proliferation of MCF-7 breast cancer cells with an IC(50) of 15 microM. There was no cross-reactivity of passiflin with anti-beta-lactoglobulin antiserum. Intact beta-lactoglobulin lacks antifungal and antiproliferative activities and is much smaller in molecular size than passiflin. However, it has been reported that hydrolyzed beta-lactoglobulin shows antifungal activity. The data suggest that passiflin is distinct from beta-lactoglobulin.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Plantas
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Neoplasias da Mama
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Extratos Vegetais
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Passiflora
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Fungos
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Lactoglobulinas
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Antifúngicos
Limite:
Animals
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Humans
Idioma:
En
Revista:
Phytomedicine
Ano de publicação:
2009
Tipo de documento:
Article