Journal
BIOANALYSIS
Volume 9, Issue 18, Pages 1361-1372Publisher
FUTURE SCI LTD
DOI: 10.4155/bio-2017-0086
Keywords
O-glycosylation heterogeneity; rFIX; recombinant coagulation factor IX; site-specific profiling
Funding
- National Research Foundation of Korea [NRF-2013M3A9B6075933]
- National Research Foundation of Korea [2013M3A9B6075933] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Ask authors/readers for more resources
Recombinant coagulation factor IX (rFIX) has extraordinarily multiple post-translational modifications including N-glycosylation and O-glycosylation which have a drastic effect on biological functions and in vivo recovery. Unlike N-glycosylation extensively characterized, there are a few studies on O-glycosylation due to its intrinsic complexity. In-depth O-glycosylation analysis is necessary to better understand and assess pharmacological activity of rFIX. Results: We determined unusual O-glycosylations including O-fucosylation and O-glucosylation which were located at Serine 53 and 61, respectively in EGF domain. Other O-glycosylations bearing core 1 glycan moiety were found on activation peptide. Conclusion: This is the first comprehensive study to characterize O-glycosylation of rFIX using MS-based glycomic and glycoproteomic approaches. Site-specific profiling will be a powerful platform to determine bioequivalence of biosimilars.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available