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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
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
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
2008-10-16 16:24:40
date last changed
2017-01-01 06:02:39
@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},
  keyword      = {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},
  volume       = {1202},
  year         = {2008},
}