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Please use this identifier to cite or link to this item: http://eprint.iitd.ac.in/handle/2074/1371

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dc.contributor.authorJain, Sulakshana-
dc.contributor.authorSingh, Rajni-
dc.contributor.authorGupta, M N-
dc.date.accessioned2006-02-22T03:48:12Z-
dc.date.available2006-02-22T03:48:12Z-
dc.date.issued2004-
dc.identifier.citationJournal of Chromatography A, 1035(1), 83-86en
dc.identifier.urihttp://eprint.iitd.ac.in/dspace/handle/2074/1371-
dc.description.abstractThe technique of three-phase partitioning (TPP) was used to purify the green fluorescent protein (GFP) in a single step. TPP uses a combination of ammonium sulphate and tert-butanol to precipitate proteins from their crude extracts. In the first round of TPP with 20% ammonium sulphate saturation at the ratio of crude to tert-butanol 1:1 (v/v), most of the GFP remains in the lower aqueous phase. When subjected to a second round of TPP with 60% ammonium sulphate saturation at the ratio of crude to tert-butanol 1:2 (v/v) gives 78% recovery of GFP with a 20-fold purification. The sodium dodecyl sulphate–polyacrylamide gel electrophoretic (SDS–PAGE) analysis of purified preparation shows single band. The fluorescence excitation and emission spectra agreed with values reported in literature.en
dc.format.extent410833 bytes-
dc.format.mimetypeapplication/pdf-
dc.language.isoenen
dc.subjectThree-phase partitioningen
dc.subjectGreen fluorescent proteinen
dc.subjectProteinsen
dc.titlePurification of recombinant green fluorescent protein by three-phase partitioningen
dc.typeArticleen
Appears in Collections:Chemistry

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