Purification of a ribosome-inactivating protein with antioxidation and root developer potencies from .

Considering as a potent antiviral plant, the attempt was made to determine, purify and characterize its proteinaceous antiviral elements against tobacco mosaic virus hypersensitive response on . By using 60% ammonium sulphate-precipitation, FPLC-based anion and cation-exchange chromatography in 10 and 50 mM NaCl, size-exclusion chromatography in 50 mM NaCl and SDS-PAGE 10%, a 25 kD antiviral protein with ribosome-inactivating/28S rRNase ability was purified from the leaves of . at vegetative growth stage. The purified protein showed FRAP-based antioxidant activity in vitro and caused 1.7-fold and 1.4-fold increases in the growth rate of root system upon carborundum-based application on the root growth medium of . . The present work reports an antiviral protein with ribosome-inactivating, antioxidation and root developer potencies in as an edible or ornamental plant that may be useful in health and agricultural biotechnology in the future.