1. Differential investigations from plasma-derived and recombinant Factor IX revealed major differences in post-translational modifications of activation peptides.
- Author
-
Chevreux G, Faid V, Andre MH, Tellier Z, and Bihoreau N
- Subjects
- Animals, CHO Cells, Cricetinae, Factor IX chemistry, Factor IX immunology, Humans, Peptide Fragments chemistry, Peptide Fragments immunology, Recombinant Proteins chemistry, Recombinant Proteins immunology, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Factor IX metabolism, Peptide Fragments blood, Protein Processing, Post-Translational, Recombinant Proteins blood
- Abstract
Post-translational modifications (PTMs) located on the activation peptide (AP) of recombinant FIX (rFIX, BeneFIX(®) ) and plasma-derived FIX (pdFIX, Betafact(®) ) have been investigated by mass spectrometry to review the structural differences between these two products. Three major structural differences were pointed out. rFIX contains a low amount of phosphorylated and sulphated AP (4% for rFIX vs. 70% for pdFIX); rFIX N-glycans are only sialylated in the α2-3 linkage, whereas pdFIX N-glycans contain both type of α2-3 and α2-6 linkages, and rFIX does not contain any sialyl Lewis(X) glycoantigens contrary to pdFIX. These variations might participate in the in vivo potential different behaviours of the two molecules., (© 2012 The Author(s). Vox Sanguinis © 2012 International Society of Blood Transfusion.)
- Published
- 2013
- Full Text
- View/download PDF