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Multipurpose peptide tags for protein isolation.

Becker, Kristian LU ; Van Alstine, James and Bülow, Leif LU (2008) In Journal of Chromatography A 1202(1). p.40-46
Abstract
A multifunctional peptide tag (HYDHYD) consisting of histidine, tyrosine and aspartate residues was fused to the N-terminal ends of green fluorescent protein (GFP), lactate dehydrogenase (LDH) and human hemoglobin (Hb), proteins which were subjected to ion-exchange chromatography (IEC), aqueous two-phase system partition, immobilized metal-ion affinity chromatography (IMAC), and hydrophobic interaction chromatography (HIC). Tagged GFP was retained significantly longer (>1 column volume) in both HIC and IEC. It exhibited 3x greater partition in favor of the hydrophobic phase in a two-phase system and 96% could be bound to an IMAC column which did not bind native GFP.
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author
; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Green fluorescent protein, Hemoglobin, Lactate dehydrogenase, Aqueous two-phase system, Hydrophobic interaction chromatography, Immobilized metal-ion affinity chromatography
in
Journal of Chromatography A
volume
1202
issue
1
pages
40 - 46
publisher
Elsevier
external identifiers
  • wos:000258982600005
  • pmid:18635190
  • scopus:48949114900
  • pmid:18635190
ISSN
0021-9673
DOI
10.1016/j.chroma.2008.06.045
language
English
LU publication?
yes
id
1ddcef8e-8ca2-4acc-ab77-31215a10a5b6 (old id 1181060)
date added to LUP
2016-04-01 14:04:56
date last changed
2025-10-14 10:56:46
@article{1ddcef8e-8ca2-4acc-ab77-31215a10a5b6,
  abstract     = {{A multifunctional peptide tag (HYDHYD) consisting of histidine, tyrosine and aspartate residues was fused to the N-terminal ends of green fluorescent protein (GFP), lactate dehydrogenase (LDH) and human hemoglobin (Hb), proteins which were subjected to ion-exchange chromatography (IEC), aqueous two-phase system partition, immobilized metal-ion affinity chromatography (IMAC), and hydrophobic interaction chromatography (HIC). Tagged GFP was retained significantly longer (>1 column volume) in both HIC and IEC. It exhibited 3x greater partition in favor of the hydrophobic phase in a two-phase system and 96% could be bound to an IMAC column which did not bind native GFP.}},
  author       = {{Becker, Kristian and Van Alstine, James and Bülow, Leif}},
  issn         = {{0021-9673}},
  keywords     = {{Green fluorescent protein; Hemoglobin; Lactate dehydrogenase; Aqueous two-phase system; Hydrophobic interaction chromatography; Immobilized metal-ion affinity chromatography}},
  language     = {{eng}},
  number       = {{1}},
  pages        = {{40--46}},
  publisher    = {{Elsevier}},
  series       = {{Journal of Chromatography A}},
  title        = {{Multipurpose peptide tags for protein isolation.}},
  url          = {{http://dx.doi.org/10.1016/j.chroma.2008.06.045}},
  doi          = {{10.1016/j.chroma.2008.06.045}},
  volume       = {{1202}},
  year         = {{2008}},
}