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http://hdl.handle.net/2074/1371
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| DC Field | Value | Language |
| contributor.author | Jain, Sulakshana | - |
| contributor.author | Singh, Rajni | - |
| contributor.author | Gupta, M N | - |
| date.accessioned | 2006-02-22T03:48:12Z | - |
| date.available | 2006-02-22T03:48:12Z | - |
| date.issued | 2004 | - |
| identifier.citation | Journal of Chromatography A, 1035(1), 83-86 | en |
| identifier.uri | http://eprint.iitd.ac.in/dspace/handle/2074/1371 | - |
| description.abstract | The 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 |
| format.extent | 410833 bytes | - |
| format.mimetype | application/pdf | - |
| language.iso | en | en |
| subject | Three-phase partitioning | en |
| subject | Green fluorescent protein | en |
| subject | Proteins | en |
| title | Purification of recombinant green fluorescent protein by three-phase partitioning | en |
| type | Article | en |
| Appears in Collections: | Chemistry
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| jainpur2004.pdf | | 401Kb | Adobe PDF | View/Open |
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