|
Abstract Abstract A 25 kD antifungal protein was extracted from Coix lacryma-jobi by ammonium sulfate precipitation, cation exchange chromatography, affinity chromatography, gel filtration and reverse-phase HPLC, respectively. Its purity was identified to be 98.23% by HPLC. The molecular weight was determined to be 25 kD by SDS-PAGE. It inhibited mycelial growth in a number of fungal species including Alternaria alternate, Trichoderma viride, and Fusarium graminearum, with an IC50 value of 9.15, 4.50 and 12.21 μmol/L, respectively. Transmission electron microscopy of mycelial of Alternaria alternate revealed marked ultrastructural changes, which included cell wall thickening and deformation, plasmolysis, cell wall perforated, cell content exudated and cell organelle severely damaged.
|
|
Received: 19 January 2009
|
|
|
|
