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Expression and purification of recombinant neurotensin in Escherichia coli.

Abstract:

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 ...

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Publication status:
Published

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Publisher copy:
10.1006/prep.2000.1246

Authors


Williamson, PT More by this author
Haddingham, T More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Journal:
Protein expression and purification
Volume:
19
Issue:
2
Pages:
271-275
Publication date:
2000-07-05
DOI:
EISSN:
1096-0279
ISSN:
1046-5928
URN:
uuid:f5d6a983-847f-480b-bbea-412f558cd8cb
Source identifiers:
99789
Local pid:
pubs:99789

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