Abstract:
:A 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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Kille P,Winge DR,Harwood JL,Kay Jdoi
10.1016/0014-5793(91)81411-zsubject
Has Abstractpub_date
1991-12-16 00:00:00pages
171-5issue
1-3eissn
0014-5793issn
1873-3468pii
0014-5793(91)81411-Zjournal_volume
295pub_type
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