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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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Purification of Chrysancorin, a Novel Antifungal Protein with Mitogenic Activity from Garland Chrysanthemum Seeds

Hexiang Wang / Xiu Yun Ye / Tzi Bun Ng

Citation Information: Biological Chemistry. Volume 382, Issue 6, Pages 947–951, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2001.118, June 2005

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A novel antifungal protein, designated chrysancorin, was isolated from seeds of Chrysanthemum coronarium var. spatiosum with a procedure involving ion exchange chromatography on DEAEcellulose, affinity chromatography on Affigel blue resin, ion exchange chromatography on SPSepharose and FPLCgel filtration on Superdex 75. The Nterminus of chrysancorin displays sequence similarity to the genomic sequence of chromosome 1 from Arabidopsis thaliana BAC T19E23. Chrysancorin exhibits a molecular mass of 13.4 kDa in gel filtration and SDSpolyacrylamide gel electrophoresis. It stimulates the proliferation of mouse splenocytes and inhibits the activity of human immunodeficiency virus-1 reverse transcriptase. The protein possesses antifungal activity against Botrytis cinerea, Mycosphaerella arachidicola and Physalospora piricola, but not against Rhizoctonia solani, Fusarium oxysporum and Coprinus comatus. However, we could not detect antibacterial activity against a variety of bacteria.

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