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Application of a pH responsive multimodal hydrophobic interaction chromatography medium for the analysis of glycosylated proteins.

Kallberg, Kristian LU ; Becker, Kristian LU and Bülow, Leif LU (2011) In Journal of chromatography. A 128(5). p.678-683
Abstract
Protein glycosylation has significant effects on the structure and function of proteins. The efficient separation and enrichment of glycoproteins from complex biological samples is one key aspect and represents a major bottleneck of glycoproteome research. In this paper, we have explored pH multimodal hydrophobic interaction chromatography to separate glycosylated from non-glycosylated forms of proteins. Three different proteins, ribonuclease, invertase and IgG, have been examined and different glycoforms have been identified. The media itself shows strong responsiveness to small variations in pH, which makes it possible to fine-tune the chromatographic conditions according to the properties of the protein isolated. Optimal glycoprotein... (More)
Protein glycosylation has significant effects on the structure and function of proteins. The efficient separation and enrichment of glycoproteins from complex biological samples is one key aspect and represents a major bottleneck of glycoproteome research. In this paper, we have explored pH multimodal hydrophobic interaction chromatography to separate glycosylated from non-glycosylated forms of proteins. Three different proteins, ribonuclease, invertase and IgG, have been examined and different glycoforms have been identified. The media itself shows strong responsiveness to small variations in pH, which makes it possible to fine-tune the chromatographic conditions according to the properties of the protein isolated. Optimal glycoprotein separation has been obtained at pH 4. The pH responsive multimodal HIC medium in contrast to conventional HIC media is able to resolve contaminating DNA. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of chromatography. A
volume
128
issue
5
pages
678 - 683
publisher
Elsevier
external identifiers
  • wos:000286848700006
  • pmid:21185570
  • scopus:78650949112
ISSN
1873-3778
DOI
10.1016/j.chroma.2010.11.080
language
English
LU publication?
yes
id
39ac3840-8a73-417c-86a0-0a8d821b07ea (old id 1755796)
date added to LUP
2011-01-11 14:59:16
date last changed
2017-10-22 04:04:17
@article{39ac3840-8a73-417c-86a0-0a8d821b07ea,
  abstract     = {Protein glycosylation has significant effects on the structure and function of proteins. The efficient separation and enrichment of glycoproteins from complex biological samples is one key aspect and represents a major bottleneck of glycoproteome research. In this paper, we have explored pH multimodal hydrophobic interaction chromatography to separate glycosylated from non-glycosylated forms of proteins. Three different proteins, ribonuclease, invertase and IgG, have been examined and different glycoforms have been identified. The media itself shows strong responsiveness to small variations in pH, which makes it possible to fine-tune the chromatographic conditions according to the properties of the protein isolated. Optimal glycoprotein separation has been obtained at pH 4. The pH responsive multimodal HIC medium in contrast to conventional HIC media is able to resolve contaminating DNA.},
  author       = {Kallberg, Kristian and Becker, Kristian and Bülow, Leif},
  issn         = {1873-3778},
  language     = {eng},
  number       = {5},
  pages        = {678--683},
  publisher    = {Elsevier},
  series       = {Journal of chromatography. A},
  title        = {Application of a pH responsive multimodal hydrophobic interaction chromatography medium for the analysis of glycosylated proteins.},
  url          = {http://dx.doi.org/10.1016/j.chroma.2010.11.080},
  volume       = {128},
  year         = {2011},
}