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Expression and purification of recombinant neurotensin in Escherichia coli

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
1046-5928
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
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), 271-275. (doi:10.1006/prep.2000.1246).

Record type: Article

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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More information

Published date: July 2000
Keywords: neurotensin, protein expression, e. coli, nmr

Identifiers

Local EPrints ID: 72083
URI: https://eprints.soton.ac.uk/id/eprint/72083
ISSN: 1046-5928
PURE UUID: cc50b7ed-3e62-4afc-b2a4-a62eb652b459
ORCID for P.T.F. Williamson: ORCID iD orcid.org/0000-0002-0231-8640

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Date deposited: 20 Jan 2010
Last modified: 06 Jun 2018 12:39

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Contributors

Author: J.F. Roth
Author: T. Haddingham
Author: A. Watts

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