A Novel Method for Identifying PEGylation Sites of Protein Using Biotinylated PEG Derivatives
Journal of Pharmaceutical Sciences, ISSN: 0022-3549, Vol: 92, Issue: 1, Page: 97-103
2003
- 43Citations
- 51Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations43
- Citation Indexes43
- 43
- CrossRef39
- Captures51
- Readers51
- 51
Article Description
The identification of PEGylation sites is essential in the characterization of PEGylated therapeutic proteins. This report describes a simple and novel method of finding poly(ethylene glycol) (PEG) conjugation sites in PEGylated proteins by using a hetero-functional biotin–PEG– N -hydroxyl succinimide derivative. PEGylated lysozyme species having a biotin moiety at each PEG chain end were separated and digested by trypsin. Among the digested lysozyme fragments, biotin-terminated PEGylated peptide fragments were purified by a monomeric avidin immobilized column. Their mass was analyzed by matrix-assisted laser desorption ionization time of flight mass spectrometry, directly indicating that PEG was conjugated to lysine 33, 97, 116 residues. Reversed-phase high-pressure liquid chromatography results for the PEGylated peptide fragments exhibited that PEGylation occurred preferentially at lysine 33> lysine 97> lysine 116.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0022354916311601; http://dx.doi.org/10.1002/jps.10270; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0037223763&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/12486686; https://linkinghub.elsevier.com/retrieve/pii/S0022354916311601; https://dx.doi.org/10.1002/jps.10270
Elsevier BV
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