Abstract:
:Development of a mass spectrometric method for the unambiguous detection of doping with recombinant human erythropoietins (rhEPO) has been attempted for many years. Unfortunately, progress in this field was hampered by the unavailability of highly purified human endogenous EPOs (urinary[uhEPO], serum/plasma EPO)--a prerequisite for generating detailed mass spectrometric glycosylation data necessary for revealing significant differences between uhEPO and rhEPOs. The paper presents the worldwide first analytical data on purified human urinary EPO generated with a high resolution high accuracy mass spectrometer (LTQ-Orbitrap). The focus is on the tryptic O-glycopeptide (E117-R131) and its degree of sialic acid O-acetylation. Data are compared with results obtained from 40 rhEPO pharmaceuticals. It could be demonstrated that the O-glycopeptide of uhEPO (ca 100 IU) contains only trace amounts of mono-acetylated mono-and di-sialylated O-glycans but no other O-acetylated structures and in this respect significantly differs from all rhEPOs. Moreover, Dynepo--a rhEPO previously thought to be not O-acetylated--also contains small amounts of O-acetylations within the O-glycan structure. The results might be useful for anti-doping purposes as well as the development of EPO pharmaceuticals with closer structural similarity to the endogenous hormone.
journal_name
Drug Test Analjournal_title
Drug testing and analysisauthors
Reichel Cdoi
10.1002/dta.1563subject
Has Abstractpub_date
2013-11-01 00:00:00pages
877-89issue
11-12eissn
1942-7603issn
1942-7611journal_volume
5pub_type
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