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KMID : 0903519970400050375
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology
1997 Volume.40 No. 5 p.375 ~ p.379
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Purification and Properties of Ribosome-inactivating Proteins from the Leaves of Cucurbita moschata ＤUCHESNE
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김영태/Kim, Yeong Tae
황영수/조강진/이시명/Hwang, Young Soo/Cho, Kang Jin/Lee, Si Myung
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Abstract
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Two ribosome-inactivating proteins, PRIP 1 and PRIP 2 have been isolated from the leaves of Cucurbita moschata D_(UCHESNE). Crude extracts were purified through ammonium sulfate precipitation and column chromatography using DE-52 cellulose, S-Sepharose, FPLC Suprose 12 HR and FPLC Mono-S. The molecular weights of PRIP 1 and PRIP 2 were 31,000 and 30,500, respectively. PRIP 2 was thermostabe and maintained its activity even after the incubation of the protein at 50℃ for 30 min. In a cell free in vitro translation system using rabbit reticulocyte lysate, protein synthesis was inhibited by the addition of PRIP 1 and PRIP 2. The IC_(50), of PRIP 1 and PRIP 2 were 0.82 nM and 0.79 nM, respectively. The comparison of N-terminal amino acid sequences of the PRIP 1 and PRIP 2 with known RIPs revealed that PRIP 1 shows sequence similarity with Luffin B from Luffa cylindrica and Trichokirin from Trichosanthes kirilowii Maximowicz and PRIP 2 has sequence similarity with Momordin Ⅱ and MAP 30 from Momordica charantia.
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