Optimizing the heterologous expression of glutathione transferase.
The heterologous expression of a protein may be enhanced by silent mutations in the coding region of its corresponding DNA. This simple approach has been successfully used for optimized production of a number of glutathione-linked enzymes. For example, the yield of human glutathione transferase M2-2 was elevated by 140-fold in a clone isolated by immunoscreening of a library of plasmids with randomized synonymous codons in the 5'-segment of the region encoding the enzyme.
Mannervik
Bengt
B
Department of Biochemistry, Uppsala University Biomedical Center, Sweden.
D003001:Cloning, Molecular / Q000379:methods*; D003062:Codon; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D005786:Gene Expression Regulation; D015723:Gene Library; D005982:Glutathione Transferase / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism*
D003062:Codon; D007527:Isoenzymes; D011993:Recombinant Fusion Proteins; D005982:Glutathione Transferase