UDP-N-acetylglucosamine:N-acetylmuramoyl-(pentapeptide) pyrophosphoryl undecaprenol N-acetylglucosamine transferase from Escherichia coli: overproduction, solubilization, and purification.

@article{Crouvoisier1999UDPNacetylglucosamineNacetylmu,
  title={UDP-N-acetylglucosamine:N-acetylmuramoyl-(pentapeptide) pyrophosphoryl undecaprenol N-acetylglucosamine transferase from Escherichia coli: overproduction, solubilization, and purification.},
  author={Muriel Crouvoisier and Dominique Mengin-Lecreulx and Jean van Heijenoort},
  journal={FEBS letters},
  year={1999},
  volume={449 2-3},
  pages={289-92}
}
Plasmids for the high-level overproduction of wild-type, and C- and N-terminal His-tagged MurG N-acetylglucosaminyl transferase from Escherichia coli were constructed. In complementation tests the three forms were active in vivo. After IPTG induction, growth, spheroplast formation and lysis, overproduced MurG proteins were mainly present (90%) in the particulate fraction. Readily solubilized by CHAPS, they were purified without any detergent to over 80% purity for both His-tagged forms but only… CONTINUE READING

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