| Literature DB >> 20363267 |
Oksana V Nekrasova1, Andrey N Wulfson, Roman V Tikhonov, Sergey A Yakimov, Tatyana N Simonova, Anna I Tagvey, Dmitry A Dolgikh, Mikhail A Ostrovsky, Mikhail P Kirpichnikov.
Abstract
Unique properties of bacteriorhodopsin, namely, photochromism and high thermal stability, make this protein an attractive target for physico-chemical studies, as well as for various biotechnological applications. Using Mistic as a suitable carrier for insertion of recombinant membrane proteins into cytoplasmic membrane of Escherichia coli, we developed a system for overexpression of bacteriorhodopsin and worked out an efficient procedure for its purification and renaturation with the final yield of 120 mg/l of refolded protein, which is the highest value reported to date for bacteriorhodopsin produced in E. coli. Functional activity of recombinant bacteriorhodopsin was confirmed by spectroscopic and electrochemical assays. 2010 Elsevier B.V. All rights reserved.Entities:
Mesh：
Substances：
Year: 2010 PMID： 20363267 DOI： 10.1016/j.jbiotec.2010.03.019
Source DB: PubMed Journal: J Biotechnol ISSN： 0168-1656 Impact factor: 3.307