Issue 21, 2004
From the journal:

Chemical Communications

Intein-mediated purification of a recombinantly expressed peptide

John A. Pezza,a   Karen N. Allenb  and  Dean R. Tolan*a  

* Corresponding authors

a Department of Biology, Boston University, 5 Cummington Street, Boston, MA, USA
E-mail: tolan@bu.edu
Fax: +1 617-358-0338
Tel: +1 617-353-5310

b Department of Physiology and Biophysics, Boston University School of Medicine, 715 Albany Street, Boston, MA, USA
E-mail: allen@med-xtal.bu.edu
Fax: +1 617-638-4273
Tel: +1 617-638-4398

Abstract

A 26 amino acid peptide has successfully been purified via recombinant expression as an intein fusion protein accompanied by cleavage without the need for any exogenous proteases or cofactors, thus offering a practical, inexpensive approach to produce isotopically labelled peptides.

Graphical abstract: Intein-mediated purification of a recombinantly expressed peptide

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Article information

DOI
https://doi.org/10.1039/B407924H
Article type
Communication
Submitted
25 May 2004
Accepted
10 Aug 2004
First published
23 Sep 2004

Chem. Commun., 2004, 2412-2413

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Intein-mediated purification of a recombinantly expressed peptide

J. A. Pezza, K. N. Allen and D. R. Tolan, Chem. Commun., 2004, 2412 DOI: 10.1039/B407924H

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