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An expression system has been designed for the rapid and economic expression of recombinant neurotensin for biophysical studies. A synthetic gene for neurotensin (Glu(1)-Leu(2)-Tyr(3)-Glu(4)-Asn(5)-Lys(6)-Pro(7)-Arg(8)-Arg(9)-Pro(1 0)-Tyr(11)-Ile(12)-Leu(13)) 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.

Original publication

DOI

10.1006/prep.2000.1246

Type

Journal article

Journal

Protein Expr Purif

Publication Date

07/2000

Volume

19

Pages

271 - 275

Keywords

Chromatography, High Pressure Liquid, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Glutathione Transferase, Neurotensin, Recombinant Fusion Proteins, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization