Open AccessThe Relationship of Secretion and Activity of Recombinant Factor IX with N-Glycosylation
Author(s) -
Samira Khalilzadeh,
Jafar Vatandoost
Publication year - 2020
Publication title -
research in molecular medicine
Language(s) - English
Resource type - Journals
eISSN - 2322-1348
pISSN - 2322-133X
DOI - 10.32598/rmm.8.1.31
Subject(s) - secretion , glycosylation , recombinant dna , chemistry , medicine , biochemistry , gene
Background: Human coagulation factor IX (hFIX) is a glycoprotein with two N-glycosylation sites at the activation peptide. Since the activation peptide is removed in mature hFIX, the exact role of N-glycosylation is unclear. To investigate the role of N-glycosylation in the secretion and activity of hFIX, we inhibited N-glycosylation by tunicamycin in the stable Human Embryonic Kidney (HEK)coagulation Factor IX (FIX) cells.
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