Application of a pH responsive multimodal hydrophobic interaction chromatography medium for the analysis of glycosylated proteins.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1755796
- author
- Kallberg, Kristian LU ; Becker, Kristian LU and Bülow, Leif LU
- organization
- publishing date
- 2011
- 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
- 2016-04-01 13:16:35
- date last changed
- 2022-02-19 03:57:07
@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}},
doi = {{10.1016/j.chroma.2010.11.080}},
volume = {{128}},
year = {{2011}},
}