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Plant and Cell Physiology, 1986, Vol. 27, No. 7 1317-1325
© 1986

Article

Purification and Characterization of a Cd-Binding Complex from the Root Tissue of Water Hyacinth Cultivated in a Cd2+-Containing Medium

Masayuki Fujita and Takahiro Kawanishi

Laboratory of Food Hygienics, Faculty of Agriculture, Kagawa University Miki-cho, Kida-gun, Kagawa 761-07, Japan

A Cd-binding complex was isolated from water hyacinth root tissue by chromatography with DEAE-cellulose and Sephadex G-50 columns followed by rechromatography on another DEAE-cellulose column. The Cd-binding complex showed a shoulder at 265 nm in the UV absorption spectrum and three bands at 234 (negative), 256 nm (negative), and 277 nm (positive) in the CD spectrum. The peptide portion of the complex was composed of only glutamic acid and/or glutamine, cysteine, and glycine in a molar ratio of 10 : 10 : 4. The molecular weight of the complex was 4,000 at neutral pHs but became lower when the complex was treated with mercaptoethanol or acid, suggesting that the complex consists of multiple oligo peptides. These results indicate that water hyacinth root Cd-binding complex is identical to fission yeast Cd- BP1, composed of two each of cadystins A and B.

(Received May 16, 1986; Accepted July 14, 1986)
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