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U.S. Department of Energy
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Copper-binding protein in Mimulus guttatus

Conference ·
OSTI ID:5520836
A Cu-binding protein has been purified from the roots of Mimulus guttatus using gel permeation chromatography on Sephadex G-75 and anion exchange chromatography on DEAE Biogel A. The protein has similar properties to putative metallothioneins (MTS) purified from other angiosperms. Putative MT was estimated by measuring the relative percentage incorporation of (/sup 35/S) into fractions containing the protein after HPLC on SW 3000-gel. In the roots of both Cu-tolerant and non tolerant plants synthesis of putative MT is induced by increased Cu concentration in the nutrient solution. The relative percentage incorporation of (/sup 35/S) into putative MT is significantly higher in extracts from the roots of Cu-tolerant than non tolerant M. guttatus after growth in 1 ..mu..M Cu suggesting involvement in the mechanism of tolerance. 22 refs., 2 figs., 1 tab.
Research Organization:
Los Alamos National Lab., NM (USA); Liverpool Univ. (UK)
DOE Contract Number:
W-7405-ENG-36
OSTI ID:
5520836
Report Number(s):
LA-UR-85-2175; CONF-850943-2; ON: DE85014094
Country of Publication:
United States
Language:
English