Cytoplasmic expression of a soluble synthetic mammalian metallothionein-α domain in Escherichia coli: Enhanced tolerance and accumulation of cadmium

Applied Biochemistry and Biotechnology - Part B Molecular Biotechnology

Volumn 16, Issue 3, 2000, Pages 211-219

  Li, Y ^a   Cockburn, W ^a   Kilpatrick, J ^a   Whitelam, G C ^a  

^a UNIVERSITY OF LEICESTER   (United Kingdom)

Author keywords

Cadmium; Fusion; Maltose binding protein; Metal binding protein; Protein expression

Indexed keywords

CADMIUM; HEAVY METAL; HYBRID PROTEIN; MALTOSE BINDING PROTEIN; METALLOTHIONEIN;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL VIABILITY; CONTROLLED STUDY; CYTOPLASM; ESCHERICHIA COLI; NONHUMAN; PROTEIN DOMAIN; PROTEIN EXPRESSION;

AMINO ACID SEQUENCE; ATP-BINDING CASSETTE TRANSPORTERS; BASE SEQUENCE; CADMIUM; CARRIER PROTEINS; CLONING, MOLECULAR; DNA, RECOMBINANT; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENE EXPRESSION; KINETICS; METALLOTHIONEIN; MOLECULAR SEQUENCE DATA; MONOSACCHARIDE TRANSPORT PROTEINS; PLASMIDS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SOLUBILITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; MAMMALIA;

EID: 0034466827     PISSN: 10736085     EISSN: None     Source Type: Journal    
DOI: 10.1385/MB:16:3:211     Document Type: Article

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