Article ID Journal Published Year Pages File Type
1176386 Analytical Biochemistry 2008 6 Pages PDF
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 PEG40K-, PEG43.5K-, and PEG47K-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.

Related Topics
Physical Sciences and Engineering Chemistry Analytical Chemistry
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