Abstract
A proteinous factor inhibiting the growth of the adzuki bean weevil (Callosobruchus chinensis L.) was separated from the seeds of Vigna mungo L. Hepper (urd bean), by sequential fractionations with ammonium sulfate, chromatographies on DEAE-cellulose, hydroxyapatite and Q-Sepharose columns. The proteinous factor was further purified to homogeneity by chromatography with a Mono-P column. The purified factor was a 40-kDa single polypeptide, as determined by SDS-PAGE, and heat-1abile but stable over a pH range from 4 to 6. It is noteworthy that this factor showed neither α-amylase and protease inhibitor activities nor lectin activity, in contrast to other growth inhibitors with those activities against bean weevils. The growth inhibitory activity was lost by respective digestions with α-chymotrypsin and subtilisin, indicating that the 40-kDa protein was a novel growth inhibitor in urd beans against the adzuki bean weevil.
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