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Immobilised peptide displaying phages as affinity ligands purification of lactoferrin from defatted milk

Noppe, W ; Plieva, Fatima LU ; Galaev, Igor LU ; Vanhoorelbeke, K ; Mattiasson, Bo LU and Deckmyn, H (2006) In Journal of Chromatography A 1101(1-2). p.79-85
Abstract
An affinity purification procedure for the direct purification of lactoferrin from defatted (skimmed) milk has been developed. The procedure is based on using selected phage clones expressing a peptide with high binding affinity for lactoferrin which were covalently coupled to macroporous poly(dimethylacrylamide) monolithic column. Large pore size (10-100 mu m) of macroporous poly(dimethylacrylamide) makes it possible to couple long (1 mu m) phage particles as ligands without any risk of blocking the monolithic column. Bound lactoferrin was eluted using 1 M NaC1 with a purity of > 95%. The technique presents a good alternative to conventional immunoaffinity chromatography for purification of a protein of interest from complex samples... (More)
An affinity purification procedure for the direct purification of lactoferrin from defatted (skimmed) milk has been developed. The procedure is based on using selected phage clones expressing a peptide with high binding affinity for lactoferrin which were covalently coupled to macroporous poly(dimethylacrylamide) monolithic column. Large pore size (10-100 mu m) of macroporous poly(dimethylacrylamide) makes it possible to couple long (1 mu m) phage particles as ligands without any risk of blocking the monolithic column. Bound lactoferrin was eluted using 1 M NaC1 with a purity of > 95%. The technique presents a good alternative to conventional immunoaffinity chromatography for purification of a protein of interest from complex samples due to (i) the robustness of the system in terms of recovery and ligand leakage and (ii) economical aspect in terms of low ligand cost. (Less)
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author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
purification, lactoferrin, macroporous monolithic gels, phage clones
in
Journal of Chromatography A
volume
1101
issue
1-2
pages
79 - 85
publisher
Elsevier
external identifiers
  • pmid:16216254
  • wos:000234639600009
  • scopus:28944452854
ISSN
0021-9673
DOI
10.1016/j.chroma.2005.09.064
language
English
LU publication?
yes
id
17c4548e-0aa9-4ddc-b314-77662a3d6303 (old id 421315)
date added to LUP
2016-04-01 17:11:52
date last changed
2021-02-17 05:21:48
@article{17c4548e-0aa9-4ddc-b314-77662a3d6303,
  abstract     = {An affinity purification procedure for the direct purification of lactoferrin from defatted (skimmed) milk has been developed. The procedure is based on using selected phage clones expressing a peptide with high binding affinity for lactoferrin which were covalently coupled to macroporous poly(dimethylacrylamide) monolithic column. Large pore size (10-100 mu m) of macroporous poly(dimethylacrylamide) makes it possible to couple long (1 mu m) phage particles as ligands without any risk of blocking the monolithic column. Bound lactoferrin was eluted using 1 M NaC1 with a purity of > 95%. The technique presents a good alternative to conventional immunoaffinity chromatography for purification of a protein of interest from complex samples due to (i) the robustness of the system in terms of recovery and ligand leakage and (ii) economical aspect in terms of low ligand cost.},
  author       = {Noppe, W and Plieva, Fatima and Galaev, Igor and Vanhoorelbeke, K and Mattiasson, Bo and Deckmyn, H},
  issn         = {0021-9673},
  language     = {eng},
  number       = {1-2},
  pages        = {79--85},
  publisher    = {Elsevier},
  series       = {Journal of Chromatography A},
  title        = {Immobilised peptide displaying phages as affinity ligands purification of lactoferrin from defatted milk},
  url          = {http://dx.doi.org/10.1016/j.chroma.2005.09.064},
  doi          = {10.1016/j.chroma.2005.09.064},
  volume       = {1101},
  year         = {2006},
}