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pubmed-article:1765150pubmed:abstractTextA metallothionein cDNA was generated from pea (Pisum sativum L.) roots, amplified by PCR and inserted into a plasmid for expression in E. coli. Purification of the resultant product generated 3 pools of cadmium-containing material after DEAE-cellulose chromatography. The amino acid composition of each was in excellent agreement with that predicted for pea metallothionein. A cadmium content of approximately 6 g.atoms per mole of protein was estimated. N-terminal sequence analysis revealed that the recombinant molecule had been proteolysed within the extended region linking the 2 cysteine-rich (putative) metal-binding regions. The significance of these findings in terms of the protein folding/targeting of the molecule are considered.lld:pubmed
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pubmed-article:1765150pubmed:articleTitleA plant metallothionein produced in E. coli.lld:pubmed
pubmed-article:1765150pubmed:affiliationDepartment of Biochemistry, University of Wales College of Cardiff, UK.lld:pubmed
pubmed-article:1765150pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1765150pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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