Premium
Differential investigations from plasma‐derived and recombinant Factor IX revealed major differences in post‐translational modifications of activation peptides
Author(s) -
Chevreux G.,
Faid V.,
Andre M.H.,
Tellier Z.,
Bihoreau N.
Publication year - 2013
Publication title -
vox sanguinis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.68
H-Index - 83
eISSN - 1423-0410
pISSN - 0042-9007
DOI - 10.1111/j.1423-0410.2012.01649.x
Subject(s) - recombinant dna , chemistry , glycan , peptide , posttranslational modification , in vivo , mass spectrometry , biochemistry , biophysics , glycoprotein , gene , chromatography , biology , genetics , enzyme
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.