Capillary electrophoretic separation of high-molecular-weight poly(ethylene glycol)-modified proteins
- Authors
- Na, DH[Na, Dong Hee]; Park, EJ[Park, Eun Ji]; Jo, YW[Jo, Yeong Woo]; Lee, KC[Lee, Kang Choon]
- Issue Date
- 15-Feb-2008
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- PEGylation; capillary electrophoresis; interferon alpha; branched PEG
- Citation
- ANALYTICAL BIOCHEMISTRY, v.373, no.2, pp.207 - 212
- Indexed
- SCIE
SCOPUS
- Journal Title
- ANALYTICAL BIOCHEMISTRY
- Volume
- 373
- Number
- 2
- Start Page
- 207
- End Page
- 212
- URI
- https://scholarworks.bwise.kr/skku/handle/2021.sw.skku/82006
- DOI
- 10.1016/j.ab.2007.08.013
- ISSN
- 0003-2697
- Abstract
- This Study was designed to demonstrate the utility of capillary electrophoresis (CE) for separating high-molecular-weight poly(ethylene glycol) (PEG)-conjugated proteins. As a CE method, sodium dodecyl sulfate-capillary gel electrophoresis (SDS-CGE) was applied to analyze interferon alpha (IFN) modified with branched and trimer-structured PEG molecules. Five mono-PEG-IFN conjugates prepared with two branched PEGs (MW 20 and 40 kDa) and three trimer-structured PEGs (MW 23.5, 43.5, and 47 kDa) were purified by cation-exchange chromatography and their masses were identified by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The SDS-CGE method showed high separation capacity by differentiating PEG-IFN conjugates with small differences in molecular size, such as PEG(40K-), PEG(43.5K-), and PEG(47K)-IFNs, and it was useful for checking the purity of each mono-PEG-IFN. This study shows that SDS-CGE can well be utilized in the development and quality control of PEGylated proteins prepared with various types of PEG. (C) 2007 Elsevier Inc. All rights reserved.
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Collections - Pharmacy > Department of Pharmacy > 1. Journal Articles
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