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Periplasmic Expression of Biologically Active Vesicular Stomatitis Virus Phosphoprotein P inEscherichia coli
Overexpression of a clone of vesicular stomatitis virus phosphoprotein P (New Jersey serotype) using T7 promoter withphoAleader sequence and a simpler two-step purification procedure of the expressed protein has been developed. The purified protein retains its ability to activate the transcription r...
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Published in: | Protein expression and purification 1996-06, Vol.7 (4), p.384-388 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Citations: | Items that cite this one |
Online Access: | Get full text |
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Summary: | Overexpression of a clone of vesicular stomatitis virus phosphoprotein P (New Jersey serotype) using T7 promoter withphoAleader sequence and a simpler two-step purification procedure of the expressed protein has been developed. The purified protein retains its ability to activate the transcription reaction. Comparative transcriptional assay using the protein P purified from periplasmic space and from cytosol (in the form of inclusion body) ofEscherichia coliestablishes the fact that the former is 10 times more efficient than the latter in activating the transcription reactionin vitro. |
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ISSN: | 1046-5928 1096-0279 |
DOI: | 10.1006/prep.1996.0057 |