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KMID : 0903519950380060528
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology
1995 Volume.38 No. 6 p.528 ~ p.533
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Purification and Characterization of Antiviral Protein(AAP29) from the Leaves of Amaranthus mangostanus
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김영태/Kim, Yeong Tae
황영수/조강진/이승인/Hwang, Young Soo/Cho, Kang Jin/Yi, Seung In
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Abstract
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An antiviral protein (AAP29) with ribosome-inactivating activity was purified and characterized from the leaves of the Amaranthus mangostanus. Purification was accomplished through crude extraction, ammonium sulfate precipitation, S-Sepharose chromatography, gel filtration, CM-Sepharose chromatography and Blue sepharose chromatography. This protein was about 29.2 kDa and strongly basic with the PI value between 9.0 and 9.6, indicating that AAP29 is similar to Type 1 RIP. The AAP29 showed high thermostability without activity toss even after 20 min at 50℃. In cell free system using rabbit reticulocyte lysate, AAP29 inhibited protein synthesis with an IC_(50), of 0.18 nM. This protein also reduced mosaic symptoms of cucumber mosaic virus (CMV) on tobacco leaves. The N-terminal amino acid sequences of the AAP29 are ADLTFTVTKDGTSQSYXTLXNXWRXW and shows no suquence similarity with any known RIPS.
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