dc.contributor.author |
Ly, Kien |
en |
dc.contributor.author |
O'Ryan, Liam |
en |
dc.contributor.author |
Mitra, Alok |
en |
dc.date.accessioned |
2018-10-10T22:49:52Z |
en |
dc.date.issued |
2015-04 |
en |
dc.identifier.issn |
1046-5928 |
en |
dc.identifier.uri |
http://hdl.handle.net/2292/40590 |
en |
dc.description.abstract |
Mercury resistance is the most widespread of all anti-microbial resistance occurring in a wide variety of Gram-negative and Gram-positive bacterial genera. The systems that are most studied and best understood are those encoded in mercury resistance (Mer) operons in Gram-negative bacteria. The mercury detoxification functions by the importation of highly toxic Hg(2+) into cytoplasm and enzymic reduction to volatile Hg(0). MerT is a small (13kDa) inner membrane protein involved in mercuric ion transport system. We have overexpressed recombinant 6His-tagged MerT from Escherichia coli in a native folded form and purified it to homogeneity in n-dodecyl-β-d-maltopyranoside (DDM) by immobilized metal affinity chromatography (IMAC). Circular dichroism showed that the protein is largely α-helical. Size-exclusion chromatography (SEC) in a variety of detergents showed that the protein exists in a multiple of oligomeric states as also confirmed by SEC coupled with multiple-angle light scattering. |
en |
dc.format.medium |
Print-Electronic |
en |
dc.language |
eng |
en |
dc.relation.ispartofseries |
Protein expression and purification |
en |
dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. |
en |
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
en |
dc.subject |
Escherichia coli |
en |
dc.subject |
Maltose |
en |
dc.subject |
Bacterial Proteins |
en |
dc.subject |
Cation Transport Proteins |
en |
dc.subject |
Recombinant Proteins |
en |
dc.title |
Overexpression, purification and biophysical characterisation of E. coli MerT. |
en |
dc.type |
Journal Article |
en |
dc.identifier.doi |
10.1016/j.pep.2014.11.016 |
en |
pubs.begin-page |
85 |
en |
pubs.volume |
108 |
en |
dc.rights.holder |
Copyright: The author |
en |
dc.identifier.pmid |
25481577 |
en |
pubs.end-page |
89 |
en |
pubs.publication-status |
Published |
en |
dc.rights.accessrights |
http://purl.org/eprint/accessRights/RestrictedAccess |
en |
pubs.subtype |
Journal Article |
en |
pubs.elements-id |
502102 |
en |
pubs.org-id |
Science |
en |
pubs.org-id |
Biological Sciences |
en |
pubs.org-id |
Science Research |
en |
pubs.org-id |
Maurice Wilkins Centre (2010-2014) |
en |
dc.identifier.eissn |
1096-0279 |
en |
pubs.record-created-at-source-date |
2015-03-17 |
en |
pubs.dimensions-id |
25481577 |
en |