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

M.B. Khazaeli | Zendy; R S Mitra | Zendy

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

Author(s) -

M.B. Khazaeli,

R S Mitra

Publication year - 1981

Publication title -

applied and environmental microbiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.552

H-Index - 324

eISSN - 1070-6291

pISSN - 0099-2240

DOI - 10.1128/aem.41.1.46-50.1981

Subject(s) - metallothionein , escherichia coli , sephadex , cadmium , chemistry , affinity chromatography , chromatography , chelation , ion chromatography , gel permeation chromatography , metal , polyacrylamide gel electrophoresis , gel electrophoresis , biochemistry , enzyme , inorganic chemistry , organic chemistry , gene , polymer

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.

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