Expression and purification of recombinant neurotensin in Escherichia coli
Expression and purification of recombinant neurotensin in Escherichia coli
An expression system has been designed for the rapid and economic expression of recombinant neurotensin for biophysical studies. A synthetic gene for neurotensin (Glu1-Leu2-Tyr3-Glu4-Asn5-Lys6-Pro7-Arg8-Arg9-Pro10-Tyr11-Ile12-Leu13) was cloned into the pGEX-5X-2 vector to allow expression of neurotensin as a glutathione S-transferase (GST) fusion protein. The inclusion of a methionine residue between the glutathione S-transferase and the neurotensin has facilitated the rapid cleavage of the neurotensin from its carrier protein. Purification of recombinant neurotensin was performed by reverse-phase HPLC. This method produced a relatively high yield of peptide and offers the potential for economic partial or uniform labeling of small peptides (<15 amino acids) with isotopes for NMR or other biophysical techniques
neurotensin, protein expression, e. coli, nmr
271-275
Williamson, P.T.F.
0b7715c6-b60e-4e95-a1b1-6afc8b9f372a
Roth, J.F.
d3e2c346-2d0b-418f-8a3c-d127a383a2b2
Haddingham, T.
1c0cc2a3-2825-4b64-aeea-c440457a58b6
Watts, A.
9d52521b-918a-4f29-aaa7-c2c3f386696f
July 2000
Williamson, P.T.F.
0b7715c6-b60e-4e95-a1b1-6afc8b9f372a
Roth, J.F.
d3e2c346-2d0b-418f-8a3c-d127a383a2b2
Haddingham, T.
1c0cc2a3-2825-4b64-aeea-c440457a58b6
Watts, A.
9d52521b-918a-4f29-aaa7-c2c3f386696f
Williamson, P.T.F., Roth, J.F., Haddingham, T. and Watts, A.
(2000)
Expression and purification of recombinant neurotensin in Escherichia coli.
Protein Expression and Purification, 19 (2), .
(doi:10.1006/prep.2000.1246).
Abstract
An expression system has been designed for the rapid and economic expression of recombinant neurotensin for biophysical studies. A synthetic gene for neurotensin (Glu1-Leu2-Tyr3-Glu4-Asn5-Lys6-Pro7-Arg8-Arg9-Pro10-Tyr11-Ile12-Leu13) was cloned into the pGEX-5X-2 vector to allow expression of neurotensin as a glutathione S-transferase (GST) fusion protein. The inclusion of a methionine residue between the glutathione S-transferase and the neurotensin has facilitated the rapid cleavage of the neurotensin from its carrier protein. Purification of recombinant neurotensin was performed by reverse-phase HPLC. This method produced a relatively high yield of peptide and offers the potential for economic partial or uniform labeling of small peptides (<15 amino acids) with isotopes for NMR or other biophysical techniques
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Published date: July 2000
Keywords:
neurotensin, protein expression, e. coli, nmr
Identifiers
Local EPrints ID: 72083
URI: http://eprints.soton.ac.uk/id/eprint/72083
ISSN: 1046-5928
PURE UUID: cc50b7ed-3e62-4afc-b2a4-a62eb652b459
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Date deposited: 20 Jan 2010
Last modified: 14 Mar 2024 02:52
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Author:
J.F. Roth
Author:
T. Haddingham
Author:
A. Watts
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