title: Intein-mediated purification of a recombinantly expressed peptide.
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.
authors.affiliation: Department of Biology, Boston University, 5 Cummington Street, Boston, MA, USA.
authors.forename: John A
authors.initials: JA
authors.lastname: Pezza
authors.forename: Karen N
authors.initials: KN
authors.lastname: Allen
authors.forename: Dean R
authors.initials: DR
authors.lastname: Tolan
mesh_terms: D006863:Hydrogen-Ion Concentration; D047668:Inteins; D010455:Peptides / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D013696:Temperature
chemical_list: D010455:Peptides; D011993:Recombinant Fusion Proteins