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Titolo:
A potent antifungal protein from Helianthus annuus flowers is a trypsin inhibitor
Autore:
Giudici, AM; Regente, MC; de la Canal, L;
Indirizzi:
Univ Mar del Plata, Inst Invest Biol, RA-7600 Mar Del Plata, Argentina Univ Mar del Plata Mar Del Plata Argentina RA-7600 Del Plata, Argentina
Titolo Testata:
PLANT PHYSIOLOGY AND BIOCHEMISTRY
fascicolo: 11, volume: 38, anno: 2000,
pagine: 881 - 888
SICI:
0981-9428(200011)38:11<881:APAPFH>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
PATHOGENESIS-RELATED PROTEINS; SCLEROTINIA-SCLEROTIORUM; ANTIMICROBIAL PEPTIDES; ASPERGILLUS-FLAVUS; PR PROTEINS; TOBACCO; PLANTS; EXPRESSION; GENES; BETA-1,3-GLUCANASE;
Keywords:
antifungal protein; plant defense; Sclerotinia sclerotiorum; sunflower; trypsin inhibitor;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: de la Canal, L Univ Mar del Plata, Inst Invest Biol, Casilla Correo 1245, RA-7600 Mar DelPlata, Argentina Univ Mar del Plata Casilla Correo 1245 Mar Del Plata Argentina RA-7600
Citazione:
A.M. Giudici et al., "A potent antifungal protein from Helianthus annuus flowers is a trypsin inhibitor", PL PHYS BIO, 38(11), 2000, pp. 881-888

Abstract

A 16-kDa protein was isolated from Helianthus annuus flowers by its ability to inhibit the germination of fungal spores. This protein, SAP16, displays an associated activity of trypsin inhibitor and was further purified to apparent homogeneity by affinity chromatography on trypsin-agarose. SAP16 causes the complete inhibition of Sclerotinia sclerotiorum ascospores germination at a concentration of 5 mug.mL(-1) (0.31 muM) and a clear reduction ofmycelial growth at lower concentrations, indicating a strong antifungal potency against this natural pathogen of sunflower. Our data suggest that theantifungal ability of SAP16 would not be the result of the inhibition of afungal protease. This study contributes to the characterization of the emerging family of antifungal proteins with an associated activity of trypsin inhibition and emphasizes their role in plant resistance against fungal attack. (C) 2000 Editions scientifiques et medicales Elsevier SAS.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/03/20 alle ore 09:17:40