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Purification, characterization and antifungal properties of a lipid‐transfer protein from sunflower ( Helianthus annuus ) seeds
Author(s) -
Regente Mariana C.,
De La Canal Laura
Publication year - 2000
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1034/j.1399-3054.2000.110203.x
Subject(s) - helianthus annuus , sunflower , plant lipid transfer proteins , size exclusion chromatography , fusarium solani , spore germination , molecular mass , biology , fusarium , biochemistry , spore , botany , chromatography , chemistry , horticulture , enzyme , gene
An antifungal protein from Helianthus annuus L. seeds (Ha‐AP10) has been purified to homogeneity and characterized. Ha‐AP10 purification was performed by gel filtration, cation exchange chromatography and reverse phase HPLC. Its molecular mass was estimated to be 10 kDa and western blot analyses suggest that it has an extracellular location. The N‐terminal sequence of Ha‐AP10 showed strong homology to some plant lipid‐transfer proteins (LTPs). Antifungal tests have demonstrated that Ha‐AP10 exerts a fungistatic effect. It completely inhibits the germination of spores of the fungal pathogen Fusarium solani f. sp. eumartii at a concentration of 40 μg ml −1 and produces a 50% growth inhibition at 6.5 μg ml −1 (0.65 μ M ). These data place Ha‐AP10 among the most potent antifungal LTPs described so far.