Purification and Partial Characterization of Antiviral Proteins from Chenopodium album L. Leaves

Two antiviral proteins from leaves of Chenopodium album L. have been purified and their characteristics compared. Both of these impart resistance in hypersensitive hosts: against tobacco mosaic virus in Nicotiana tabacum cv. Samsun NN and N. glutinosa, and sunnhemp rosette virus in Cyamopsis tetragonoloba. One of them exhibited a single polypeptide with a molecular mass of 25 kD, and the other one is a complex showing polypeptide bands of 27, 25 and 18 kD on SDS-PAGE. The 25 kD protein and the complex protein inhibited more than 90% lesion formation at a concentration of 20–22 μg mL−1. Both of the proteins are basic in nature and can tolerate high temperature (up to 90 °C).