期刊
JOURNAL OF PEPTIDE RESEARCH
卷 59, 期 5, 页码 197-202出版社
BLACKWELL MUNKSGAARD
DOI: 10.1034/j.1399-3011.2002.00978.x
关键词
bitter gourd; napin; ribosome-inactivating peptide; seeds
A peptide designated charantin, with a molecular mass of 9.7 kDa, was isolated from bitter gourd seeds. The procedure comprised affinity chromatography on Affi-gel blue gel, ion-exchange chromatography on Mono S and gel filtration on Superdex 75. The N-terminal sequence of charantin exhibited marked similarity to that of the 7.8-kDa napin-like peptide previously isolated from bitter gourd seeds. Charantin inhibited cell-free translation in a rabbit reticulocyte lysate system with an IC50 of 400 nM, a potency lower than that of the previously reported small ribosome-inactivating protein gamma-momorcharin (IC50=55 nM) which also exhibited an abundance of arginine and glutamate/glutamine residues. Charantin reacted positively in the N-glycosidase assay, yielding a band similar to that formed by the small ribosome-inactivating proteins gamma-momorcharin and luffin S.
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