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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Crouvoisier M,Mengin-Lecreulx D,van Heijenoort Jdoi
10.1016/s0014-5793(99)00412-3keywords:
subject
Has Abstractpub_date
1999-04-23 00:00:00pages
289-92issue
2-3eissn
0014-5793issn
1873-3468pii
S0014-5793(99)00412-3journal_volume
449pub_type
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