Isolation and Partial Purification of Cadmium-Binding Protein from Roots of the Grass Agrostis gigantea
- 1 April 1984
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 74 (4) , 1025-1029
- https://doi.org/10.1104/pp.74.4.1025
Abstract
A Cd-binding protein was isolated from roots of the grass A. gigantea Roth. Heat-stable proteins were chromatographed on the anion exchanger QAE-Sephadex A-25. The major Cd fraction was purified further by gel filtration on Sephadex G-75 in 1 M KCl buffer. The resulting protein preparation was light brown, had an apparent MW of 3700, contained 29% cysteine and close to 4 gram atoms Cd/mole. The Cd:cysteine ratio was 1:2.7. Spectroscopic measurements indicated Cd-thiolate coordination. The roots produced the metallothionein-like protein when they were exposed to Cd for 7 days.This publication has 9 references indexed in Scilit:
- Estimating Thiol-rich Copper-binding Protein in Small Root SamplesZeitschrift für Pflanzenphysiologie, 1983
- Characterization of isoprotein patterns in tissue extracts and isolated samples of metallothioneins by reverse-phase high-pressure liquid chromatographyBiochemical Journal, 1983
- Cadmium-Binding Components in Soybean PlantsPlant Physiology, 1982
- Inducible Cadmium Binding Complexes of Cabbage and TobaccoPlant Physiology, 1982
- Differences in the polymorphic forms of metallothioneinArchives of Biochemistry and Biophysics, 1982
- Partial Characterization of a Cadmium-binding Protein from the Roots of Cadmium-treated TomatoPlant Physiology, 1980
- Metallothionein: An Exceptional Metal Thiolate ProteinPublished by Wiley ,1980
- Circular dichroism of metallothioneinsBiochimica et Biophysica Acta (BBA) - Protein Structure, 1978
- Copper-chelatin: Isolation from various eucaryotic sourcesArchives of Biochemistry and Biophysics, 1975