Purification and properties of a membrane-bound lytic transglycosylase from Escherichia coli.

@article{Ursinus1994PurificationAP,
  title={Purification and properties of a membrane-bound lytic transglycosylase from Escherichia coli.},
  author={Astrid Ursinus and J. - V. H{\"o}ltje},
  journal={Journal of bacteriology},
  year={1994},
  volume={176 2},
  pages={338-43}
}
A membrane-bound lytic transglycosylase (Mlt) has been solubilized in the presence of 2% Triton X-100 containing 0.5 M NaCl from membranes of an Escherichia coli mutant that carries a deletion in the slt gene coding for a 70-kDa soluble lytic transglycosylase (Slt70). The enzyme was purified by a four-step procedure including anion-exchange (HiLoad SP-Sepharose and MonoS), heparin-Sepharose, and poly(U)-Sepharose 4B column chromatography. The purified protein that migrated during denaturing… CONTINUE READING

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