AI Article Synopsis
- A variant peak of recombinant human erythropoietin (rHu-EPO) was identified during RP-HPLC analysis, constituting about 7% of the total content.
- Mass analysis via ESI-TOF MS revealed that the variant peak has a molecular mass that is 600-1000 Da smaller than the main peak, indicating structural differences.
- Peptide mapping showed that the variant lacks O-glycopeptides at Ser126, leading to the conclusion that it is non-O-glycosylated rHu-EPO, while the main peak is fully O-glycosylated.
Article Abstract
A variant peak was detected in the analysis of RP-HPLC of rHu-EPO, which has about 7% relative content. Fractions of the main and the variant peaks were pooled separately and further analyzed to identify the molecular structure of the variant peak. Total mass analysis for each peak fraction using ESI-TOF MS shows differences in molecular mass. The fraction of the main peak tends to result in higher molecular masses than the fraction of the variant. The detected masses for the variant are about 600-1000 Da smaller than those for the main peak. Peptide mapping analysis for each peak fraction using Asp-N and Glu-C shows differences in O-glycopeptide profiles at Ser126. The O-glycopeptides were not detected in the fraction of the variant. It is concluded that the variant peak is non-O-glycosylated rHu-EPO and the main peak is fully O-glycosylated rHu-EPO at Ser126.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4469907 | PMC |
| http://dx.doi.org/10.14348/molcells.2015.2256 | DOI Listing |
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