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Purification of tryptophan containing synthetic peptides by selective binding of the alpha-amino group to immobilised metal ions

Hansen, P.; Lindeberg, G.

Journal of Chromatography. a 662(2): 235-241

1994

ISSN/ISBN: 0021-9673
PMID: 8143027
DOI: 10.1016/0021-9673(94)80510-5
Accession: 033041125
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Immobilised metal ion affinity chromatography (IMAC) based on selective binding via the alpha-amino group to Cu2+ and Ni2+ ions has been used to purify tryptophan containing synthetic peptides. A free alpha-amino group, serving as an affinity handle, is present only in the target peptide when the peptides are synthesised by the solid-phase method and remaining amino groups after each coupling step are blocked by acetylation. A free alpha-amino group is necessary to retain the peptide on the column. The tryptophan residue may contribute to the binding only if the peptide is simultaneously anchored via the alpha-amino group.

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Related References

Hansen, P.; Lindeberg, G. 1994: Purification of tryptophan containing synthetic peptides by selective binding of the α-amino group to immobilised metal ions Journal of Chromatography 662(2): 235-241
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