| Literature DB >> 10338150 |
M Crouvoisier1, D Mengin-Lecreulx, J van Heijenoort.
Abstract
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 up to 20% for the wild-type form. The enzymatic activity of each purified MurG protein was determined and found to be inhibited to the same extent by ramoplanin.Entities:
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Year: 1999 PMID： 10338150 DOI： 10.1016/s0014-5793(99)00412-3
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124