Multipurpose peptide tags for protein isolation.
(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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1181060
- author
- Becker, Kristian LU ; Van Alstine, James and Bülow, Leif LU
- organization
- publishing date
- 2008
- 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
- 2022-01-27 22:44:34
@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}}, }