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. 1984 Apr;74(4):1025–1029. doi: 10.1104/pp.74.4.1025

Isolation and Partial Purification of Cadmium-Binding Protein from Roots of the Grass Agrostis gigantea1

Wilfried E Rauser 1
PMCID: PMC1066812  PMID: 16663497

Abstract

A cadmium-binding protein was isolated from roots of the grass Agrostis gigantea Roth. Heat-stable proteins were chromatographed on the anion exchanger QAE-Sephadex A-25. The major cadmium fraction was purified further by gel filtration on Sephadex G-75 in 1 molar KCl buffer. The resulting protein preparation was light brown, had an apparent molecular weight of 3700, contained 29% cysteine and close to 4 gram atoms cadmium/mole. The cadmium:cysteine ratio was 1:2.7. Spectroscopic measurements indicated cadmium-thiolate coordination. The roots produced the metallothionein-like protein when they were exposed to cadmium for 7 days.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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