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Purification and Characterization of PC-Like Cadmium-Binding Peptide from Root of Rumex crispus

  • Chang, Ju-Youn (Department of Life Science, Ewha Womans University) ;
  • Lee, In-Sook (Department of Life Science, Ewha Womans University) ;
  • Park, Jin-Sung (Department of Life Science, Ewha Womans University) ;
  • Chang, Yoon-Young (Department of Environmental Engineering, Kwangwoon University) ;
  • Bae, Bum-Han (Department of Civil & Environmental Engineering, Kyungwon University)
  • Published : 2003.10.01

Abstract

This research investigated the process of removing cadmium and tested the detoxification mechanism of the cadmium-binding peptide (Cd-BP) from Rumex crispus. Phytochelatin-like cadmium-binding peptide (PC-Cd-BP) of Rumex crispus was purified and identified. Rumex crispus was exposed to 4.3 mg Cd/L for seven days. Heat-treated supernatant fraction taken by root tissues showed traces of PC-Cd-BP An analysis of the material through Gel-filteration chromatography on the Sephadex G-75 column showed two symmetrical Cd-BP peaks. The major peak with the smaller molecular weight was further purified by $C_{18}$ reverse-phase HPLC to produce apparent homogeneity. The amino acid composition of Cd-BP from Rumex crispus included cysteine (22.6%), glutamate and glutamate acid (20%), and glycine (12%). It was similar the amino acid composition of most PC. The molecular weight of the purified peptide was determined at 568-706 Da by MALDI-TOF MS. Therefore, the Cd-BP of Rumex crispus was PC-Cd-BP consisting of isopeptides.

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