Purification of a maize dehydrin protein expressed in Escherichia coli.

@article{Jepson1995PurificationOA,
  title={Purification of a maize dehydrin protein expressed in Escherichia coli.},
  author={S G Jepson and Timothy J. Close},
  journal={Protein expression and purification},
  year={1995},
  volume={6 5},
  pages={632-6}
}
A maize dehydrin protein (Dhn1) containing 167 amino acids with a predicted molecular weight of 17.0 kDa was produced in the Escherichia coli overexpression strain BL21 (DE3)pLysS. Site-directed mutagenesis was used to construct a plasmid with a protein coding region corresponding exactly to the original cDNA. Protein production was induced by IPTG. Dhn1 was enriched from total soluble protein by heat-fractionation and centrifugation and then purified by sequential cation exchange and… CONTINUE READING