Ribosome-inactivating activity and cDNA Cloning of Antiviral Protein Isoforms of Chenopodium album

We have characterized a novel type I ribosomeinactivating protein (CAP30) from the leaves of Chenopodium album. Purified native CAP30 depurinated the ribosomes of Chenopodium, tomato, and to bacco leaves in vitro. The further characterize this protein, cDNA clones were isolated from a leaf cDNA libr...

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Veröffentlicht in:	Molecules and cells 2004-02, Vol.17 (1), p.73-80
Hauptverfasser:	Park, J.S, Hwang, D.J, Lee, S.M, Kim, Y.T, Cho, K.J. (National Institute of Agricultural Biotechnology, Rural Development Administrate, Suwon, Republic of Korea), Choi, S.B. (Myongji University, Yongin, Republic of Korea)
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Antiviral Agents - pharmacology CHENOPODIUM Chenopodium album - metabolism Cloning, Molecular DNA, Complementary - metabolism Escherichia coli - metabolism Gene Library Molecular Sequence Data N-Glycosyl Hydrolases - chemistry N-Glycosyl Hydrolases - genetics Phylogeny Plant Leaves - metabolism Plant Proteins - chemistry Protein Isoforms Protein Sorting Signals Protein Structure, Tertiary Ribosome Inactivating Proteins RIBOSOMES Ribosomes - chemistry Ribosomes - metabolism RNA - chemistry Sequence Homology, Amino Acid Time Factors
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Zusammenfassung:	We have characterized a novel type I ribosomeinactivating protein (CAP30) from the leaves of Chenopodium album. Purified native CAP30 depurinated the ribosomes of Chenopodium, tomato, and to bacco leaves in vitro. The further characterize this protein, cDNA clones were isolated from a leaf cDNA library using a DNA probe derived from the N-terminal amino acid sequence.
ISSN:	1016-8478
DOI:	10.1016/S1016-8478(23)13009-3