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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Hydrogen-Ion Concentration
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Inteins*
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Peptides / chemistry*
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Peptides / genetics
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Peptides / isolation & purification*
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / isolation & purification
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Temperature
Substances
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Peptides
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Recombinant Fusion Proteins