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Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
The influence of different glycosylation patterns on factor VII biological activity
Ieva Sutkeviciute1, Edita Mistiniene, Jolanta Sereikaite
1Department of Chemistry and Bioengineering, Vilnius Gediminas Technical University, Vilnius, Lithuania. ieva.sutkeviciute@gmail.com
Abstract:
In this study the bioactivity of three differently glycosylated blood coagulation factor VII (FVII) variants (human plasma FVII, recombinant human FVII produced in CHO and BHK cell cultures) were analyzed and compared. Surface plasmon resonance studies of FVII interaction with soluble and full length TF together with FVII autoactivation assays revealed that BHK-derived FVII has the highest bioactivity, while human plasma and CHO-derived FVII showed very similar bioactivity. The affinity of FVII variants to TF correlates with FVII autoactivation rates--the higher the affinity, the faster the autoactivation rate.
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