Affinity chromatography as a means to study multienzyme complexes involved in murein synthesis.

@article{Rechenberg1996AffinityCA,
  title={Affinity chromatography as a means to study multienzyme complexes involved in murein synthesis.},
  author={Moritz von Rechenberg and Astrid Ursinus and J. - V. H{\"o}ltje},
  journal={Microbial drug resistance},
  year={1996},
  volume={2 1},
  pages={
          155-7
        }
}
The interaction of murein hydrolases and synthases was studied by affinity chromatography. The lytic transglycosylases Slt70 and MltB of E. coli were purified and covalently linked to CNBr-activated Sepharose. Membrane extracts were analyzed for proteins that interact with the immobilized murein hydrolases. Slt70-Sepharose was found to retain the PBPs 1b, 1c, 2, and 3. Likewise MltB-Sepharose enriched PBP 1b, 1c, and 3. Thus both lytic transglycosylases have an affinity for a transpeptidase… CONTINUE READING
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