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

von Rechenberg, M., Ursinus, A., & Höltje, J.-V. (1996). Affinity chromatography as a means to study multienzyme complexes involved in murein synthesis. Microbial Drug Resistance, 2(1), 155-157. doi:10.1089/mdr.1996.2.155.

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von Rechenberg, M1, Autor           
Ursinus, A1, Autor                 
Höltje, J-V1, Autor           
Affiliations:
1Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3375718              

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 Zusammenfassung: 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, PBP2 and/or 3, as well as for the bifunctional transpeptidase/transglycosylase 1b. Interestingly, in addition, the poorly characterized PBP 1c interacts strongly with both Slt70 and MltB. It is speculated that the lytic transglycosylases assemble a multienzyme complex consisting of hydrolases and synthases, which is involved in growth of the stress-bearing murein sacculus.

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 Datum: 1996-04
 Publikationsstatus: Erschienen
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 Ort, Verlag, Ausgabe: -
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 Art der Begutachtung: -
 Identifikatoren: DOI: 10.1089/mdr.1996.2.155
PMID: 9158739
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Titel: Microbial Drug Resistance
  Andere : Microbial Drug Resistance: MDR: mechanisms, epidemiology, and disease
  Kurztitel : Microb Drug Resist
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Larchmont, NY, USA : Liebert
Seiten: - Band / Heft: 2 (1) Artikelnummer: - Start- / Endseite: 155 - 157 Identifikator: ISSN: 1076-6294
CoNE: https://pure.mpg.de/cone/journals/resource/1076-6294