Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: Combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization☆
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Glycan analysis of glycoprotein pharmaceuticals: Evaluation of analytical approaches to Z number determination in pharmaceutical erythropoietin products
2011, BiologicalsCitation Excerpt :One of the rhEPO N-glycans, the tetra-sialylated tetra-antennary N-glycans had been shown as the major determinant for its in vivo biological activity [6]. Since glycosylation pattern of a recombinant glycoprotein differs in cell lines and can also be influenced by the culture conditions and downstream production processes, thus glycosylation profiling is an important parameter for product consistency and control [4,5,7–12]. The structural information of glycosylation between batches can be compared by various methodologies such as isoelectric focusing and capillary electrophoresis on intact glycoproteins.
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2006, Biochemical and Biophysical Research CommunicationsCitation Excerpt :rEpo (Roche) was run in parallel as a control. Samples adjusted to 1000 U/100 μl were boiled for 10 min, and then 0.5 μl Triton X-100 and 1 U N-glycosidase F (Roche) were added [27]. After incubating at 37 °C for various intervals (1, 2, 4, and 15 h), the reaction was stopped by boiling for 10 min and analyzed by Western blot using an anti-Epo polyclonal antibody (R&D Systems).
New urinary EPO drug testing method using two-dimensional gel electrophoresis
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Supported by NIH Research Grant DK09970 and Postdoctoral Fellowship GM13013-01 Bi-4 (K.G.R.).
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Present address: Department of Pharmaceutics and Pharmaceutical Chemistry, Ohio State University, Columbus, OH 43210.