Plant Diversity ›› 2007, Vol. 29 ›› Issue (02): 247-250.

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Biophysical and Pharmacological Characterization of a Dynamin-like Protein from Day-lily ( Hemerocallis fulva , Liliaceae) Pollens

LIAO Jun-Jie1 , 2 , WU Ying-Jie3 * * , YAN Lung-Fei1   

  1. 1 College of Biological Sciences, China Agricultural University , State Key Labratory of Plant Physiology and Biochemistry , Beijing 100094 , China; 2 Department of Food and Bio- technology , Guangdong Light Industry Technologic College, Guangzhou 510300 , China ; 3 Department of Medicine, Mount Sinai School of Medicine , New York , NY 10029 , America
  • Received:2006-05-11 Online:2007-04-25 Published:2007-04-25
  • Contact: WU Ying-Jie

Abstract:

A novel motor protein , dynamin- like protein from day lily, was purified and identified by FPLC . Here we report its biochemical characterization . The molecular weight of the dynamin-like protein is 100 kD on SDS-PAGE. Isoelectric points are about 6. 15 and 6 .80 . The fluorescence emission wave length of dynamin-like protein is 346 nm by excitation at 280 nm . Through fluorescence spectra analysis, ultraviolet absorption spectrum and derivative spectrum, we conclude that it contains tryptophan and tyrosine residues . Pharmacological study indicates that mercapto may play an important role in
enzyme activity of dynamin-like protein .

Key words: Dynamin-like protein