光谱学与光谱分析 |
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Fluorescence Spectra Study of a New Toxic Protein from Malania Oleifera |
YUAN Yan1, 2,XIAO Han1,KANG Hong-jun1,CHEN Rui-yan1,DAI Xiao-chang1* |
1. Key Laboratory of Medical Chemistry for Natural Resource, Ministry of Education, School of Chemical Science and Technology, Yunan University, Kunming 650091, China 2. Department of Life Science and Technology, Kunming University, Kunming 650031, China |
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Abstract A new toxic protein named malanin was isolated from seeds of Malania oleifera by hydrophobic chromatography, whose cytotoxic activities against carcinoma cells were very strong. The conformational changes of malanin at various temperatures, pH, organic solvents, surfactant, denaturant and fluorescence quenching solvents were studied by fluorescence spectra. The fluorescence spectra of malanin excited at 280 nm and 295 nm showed a maximum at 340 nm. The emission spectra of malanin showed that Trp residues were located by a great degree in the hydrophobic area. Addition of SDS, CH5N3·HSCN, acrylamide and KI led to changes in the molecular conformation of malanin, and caused the fluorescence quenching of Trp residues. The red-shifted emission band of malanin after adding CH5N3·HSCN showed that Trp residues were exposed in polar solvents.
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Received: 2008-02-22
Accepted: 2008-05-26
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Corresponding Authors:
DAI Xiao-chang
E-mail: xchdai@ynu.edu.cn
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