Cadmium-binding component in Escherichia coli during accommodation to low levels of this ion

Abstract

An inducible cadmium-binding protein was isolated from E. coli cells accommodated to 3x10-6 M Cd2+ but ot from normal or unaccommodated cells. Sephadex G-100, metal chelate affinity chromatography, and disc gel electrophoresis were used in the purification procedure. The molecular weight of the Cd2+-binding protein was estimated to be about 39,000 by Sephadex G-100 chromatography, making it different from the conventional, much smaller metallothionein.