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Purification and Characterization of Flammulin,a Basic Protein with Anti-tumor Activities from Flammulina velutipes

CHEN Chang, XUE Jiu-gang, ZHOU Kai-song, LI Yan, ZHANG Han-xing, ZHANG Chang-kai*   

  1. State Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, China
  • Received:2003-02-12 Revised:2003-05-10 Online:2003-06-15 Published:2003-06-15

Abstract: Aim To purify and characterize flammulin, a basic protein with anti-tumor activities. Methods Ammonium sulfate, ethanol fractionation and column chromatography were used for separation and purification. Electrophoretic analysis, amino acid analysis, and MS of flammulin were carried out. Results Flammulin was purified to electrophoretic homogeneity and crystallized. With a molecular mass of 19891.13 Da, pI = 8.9, λmax = 276-278 nm, λmin = 250nm, flammulin was characterized by its lack of methionine. Fingerprint mapping of flammulin was determined by MALDI-MS following in-gel protease digestion; no close matches were identified. Conclusion Flammulin was purified to electrophoretic neity, and its characteristics are discussed for the first time.

Key words: anti tumor activities, anti tumor activities, flammulin , flammulin , Flammulina velutipes, Flammulina velutipes, purification , purification , characterization , characterization , massspectrometry, massspectrometry

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