Abstract:
:Escherichia coli maltose-binding protein (MBP) is frequently used as an affinity tag to facilitate the purification of recombinant proteins. An important additional attribute of MBP is its remarkable ability to enhance the solubility of its fusion partners. MBPs are present in a wide variety of microorganisms including both mesophilic and thermophilic bacteria and archaea. In the present study, we compared the ability of MBPs from six diverse microorganisms (E. coli, Pyrococcus furiosus, Thermococcus litoralis, Vibrio cholerae, Thermotoga maritima, and Yersinia pestis) to promote the solubility of eight different aggregation-prone proteins in E. coli. In contrast to glutathione S-transferase (GST), all of these MBPs proved to be effective solubility enhancers and some of them were even more potent solubilizing agents than E. coli MBP.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Fox JD,Routzahn KM,Bucher MH,Waugh DSdoi
10.1016/s0014-5793(03)00070-xkeywords:
subject
Has Abstractpub_date
2003-02-27 00:00:00pages
53-7issue
1-3eissn
0014-5793issn
1873-3468pii
S001457930300070Xjournal_volume
537pub_type
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