A new method for purification of functional recombinant GST-cyclophilin A protein from E. coli.

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dc.contributor.authorLee, Seonminen_US
dc.contributor.authorHan, Xuezheen_US
dc.contributor.authorChoi, Kyu Jinen_US
dc.contributor.authorDing, Yanen_US
dc.contributor.authorChoi, Taegyuen_US
dc.contributor.authorTak, Eunyoungen_US
dc.contributor.authorLee, Jisunen_US
dc.contributor.authorHa, Joohunen_US
dc.contributor.authorKim, Sung Sooen_US
dc.contributor.authorLee, Jinhwaen_US
dc.date.accessioned2008-12-26en_US
dc.date.accessioned2009-05-27T09:24:28Z
dc.date.available2008-12-26en_US
dc.date.available2009-05-27T09:24:28Z
dc.date.issued2008-12-26en_US
dc.description.abstractThe expression of glutathione-S-transferase (GST) fusion protein is extensively utilized in the study of protein-protein interactions. In the commonly used purification method, the overexpressed GST fusion protein is bound to the glutathione (GSH)-coupled resins via affinity chromatography, and then eluted by an excessive quantity of reduced GSH. However, this technique has certain limitations, such as low product purity, retention of GSH in the sample, as well as relatively high cost. To overcome these limitations, in this study, elution buffer containing 2% formic acid was utilized rather than GSH to elute the GST-fusion protein, and thereafter the acidic samples were neutralized using collecting buffer. By using this method, highly purified GST-cyclophilin A (CypA) fusion protein was obtained, without affecting the structural and functional characteristics such as PPIase and chaperone activities. Moreover, the procedure is also cost-effective, due to the low cost of formic acid as compared with GSH.en_US
dc.description.affiliationDepartment of Biochemistry and Molecular Biology, Medical Science and Engineering Research Center for Bioreaction to Reactive Oxygen Species and Biomedical Science Institute (BK-21), School of Medicine, Kyung Hee University, Seoul 130-701, Korea.en_US
dc.identifier.citationLee S, Han X, Choi KJ, Ding Y, Choi T, Tak E, Lee J, Ha J, Kim SS, Lee J. A new method for purification of functional recombinant GST-cyclophilin A protein from E. coli. Indian Journal of Biochemistry & Biophysics. 2008 Dec; 45(6): 374-8en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/27413
dc.language.isoengen_US
dc.source.urihttps://https://www.niscair.res.in/ScienceCommunication/ResearchJournals/rejour/ijbb/ijbb0.aspen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCloning, Molecularen_US
dc.subject.meshCyclophilin A --geneticsen_US
dc.subject.meshEscherichia coli --enzymologyen_US
dc.subject.meshFormic Acids --chemistryen_US
dc.subject.meshGlutathione Transferase --geneticsen_US
dc.subject.meshMolecular Chaperones --geneticsen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshProtein Foldingen_US
dc.subject.meshRatsen_US
dc.subject.meshRecombinant Fusion Proteins --geneticsen_US
dc.titleA new method for purification of functional recombinant GST-cyclophilin A protein from E. coli.en_US
dc.typeJournal Articleen_US
dc.typeResearch Support, Non-U.S. Gov'ten_US
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