Abstract
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.
MeSH Terms
Adaptation, Physiological
Cadmium/isolation & purification,metabolism
Carrier Proteins/isolation & purification
Chromatography, Affinity
Electrophoresis, Polyacrylamide Gel
Escherichia coli/analysis,metabolism
Metalloproteins/isolation & purification
Metallothionein/isolation & purification
Molecular Weight
Chemicals
Carrier Proteins
Metalloproteins
cadmium-binding protein
Cadmium
Metallothionein
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Khazaeli M B
Mitra R S
References (14)
14 references, click to expand
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