Cadmium-binding component in Escherichia coli during accommodation to low levels of this ion.
An inducible cadmium-binding protein was isolated from Escherichia coli cells accommodated to 3 X 10(-6) M Cd2+ but not 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.
D000222:Adaptation, Physiological; D002104:Cadmium / Q000302:isolation & purification* / Q000378:metabolism*; D002352:Carrier Proteins / Q000302:isolation & purification*; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000032:analysis* / Q000378:metabolism; D008667:Metalloproteins / Q000302:isolation & purification*; D008668:Metallothionein / Q000302:isolation & purification*; D008970:Molecular Weight
D002352:Carrier Proteins; D008667:Metalloproteins; C004203:cadmium-binding protein; D002104:Cadmium; D008668:Metallothionein