Abstract
A purification scheme involving ion exchange chromatography on DEAE–cellulose, affinity chromatography on Affi-gel blue gel, and ion exchange chromatography on CM–Sepharose and Mono S was employed to isolate a peptide with a molecular weight of 7.8 kDa from sponge gourd seeds. The peptide, which was designated luffacylin, exhibited an N-terminal sequence with pronounced resemblance to that of the 6.5 kDa arginine–glutamate rich polypeptide previously isolated from sponge gourd seeds. Luffacylin inhibited translation in a rabbit reticulocyte lysate system with an ic 50 of 140 pM and reacted positively in the N-glycosidase assay for ribosome inactivating proteins. Luffacylin exerted anti-fungal activity against Mycosphaerella arachidicola and Fusarium oxysporum.
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