Differential investigations from plasma‐derived and recombinant Factor IX revealed major differences in post‐translational modifications of activation peptides. Issue 2 (10th September 2012)

• Record Type: Journal Article
• Authors: Chevreux, G.; Faid, V.; Andre, M.‐H.; Tellier, Z.; Bihoreau, N.
• Is Part Of: Vox sanguinis. Volume 104:Issue 2(2013)
• Page Start: 171
• Page End: 174
• Publication Date: 2012-09-10
• Subjects: Blood -- Periodicals; Blood -- Transfusion -- Periodicals; Immunohematology -- Periodicals; Immunopathology -- Periodicals; 615.39
• DOI: 10.1111/j.1423-0410.2012.01649.x
• Languages: English
• ISSNs: 0042-9007

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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 <italic>N</italic>‐glycans are only sialylated in the α2‐3 linkage, whereas pdFIX <italic>N</italic>‐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 <italic>in vivo</italic> potential different behaviours of the two molecules.</p> </abstract>