Abstract
A new inhibitor of plant virus infection from fruiting bodies of Lentinus edodes was purified by a method using fractionation with DEAE-Cellulose, gel filtration on Sephadex G-75, and column chromatography on CM-Toyopearl 650M. The purified inhibitor thus obtained was homogeneous on disc and SDS disc electrophoreses, and the molecular weight of the inhibitor was 23, 000. The inhibitor consisted of 17.4% nitrogen, which was found to be a basic simple protein, but contained no neutral sugar, hexosamine nor sialic acid. The inhibitor was estimated to be composed of about 199 amino acid residues. This inhibitor was named "fruiting body protein (FBP)."
