Intermediate purification of CHO-derived recombinant human Factor IX using hydrophobic interaction membrane-based chromatography and its comparison to a sulfated resin

2017 ◽  
Vol 38 (22-23) ◽  
pp. 2900-2908
Author(s):  
Daniel A. Ribeiro ◽  
Douglas F. Passos ◽  
Helen C. Ferraz ◽  
Leda R. Castilho
Keyword(s):  
Hydrophobic Interaction ◽  
Human Factor ◽  
Factor Ix ◽  
Human Factor Ix ◽  
Recombinant Human Factor Ix

A galactopoiesis accordant yield of functional recombinant human factor IX from homozygous transgenic pigs requires a large amount of vitamin K supplementation

2016 ◽  
Vol 25 (4) ◽  
pp. 545-551
Author(s):  
Chon-Ho Yen ◽  
Tien-Shuh Yang ◽  
Yin-Shen Lin ◽  
Meng-Hwan Lee ◽  
Kuo-Cheng Yu ◽  
...  
Keyword(s):  
Vitamin K ◽  
Human Factor ◽  
Factor Ix ◽  
Transgenic Pigs ◽  
Human Factor Ix ◽  
Recombinant Human Factor Ix

scholarly journals Improved Expression of Recombinant Human Factor IX by Co-expression of GGCX, VKOR and Furin

2014 ◽  
Vol 33 (2) ◽  
pp. 174-183 ◽  
Author(s):  
Jianming Liu ◽  
Anna Jonebring ◽  
Jonas Hagström ◽  
Ann-Christin Nyström ◽  
Ann Lövgren
Keyword(s):  
Human Factor ◽  
Factor Ix ◽  
Human Factor Ix ◽  
Recombinant Human Factor Ix

A prospective registry of European haemophilia B patients receiving nonacog alfa, recombinant human factor IX, for usual use

Haemophilia ◽  
2011 ◽  
Vol 18 (4) ◽  
pp. 503-509 ◽  
Author(s):  
E. BERNTORP ◽  
D. KEELING ◽  
M. MAKRIS ◽  
A. TAGLIAFERRI ◽  
C. MALE ◽  
...  
Keyword(s):  
Human Factor ◽  
Factor Ix ◽  
Haemophilia B ◽  
Human Factor Ix ◽  
Recombinant Human Factor Ix

Approaches for recombinant human factor IX production in serum-free suspension cultures

2015 ◽  
Vol 38 (3) ◽  
pp. 385-394 ◽  
Author(s):  
Robson Luis Ferraz do Amaral ◽  
Aline de Sousa Bomfim ◽  
Mário Soares de Abreu-Neto ◽  
Virgínia Picanço-Castro ◽  
Elisa Maria de Sousa Russo ◽  
...  
Keyword(s):  
Human Factor ◽  
Suspension Cultures ◽  
Factor Ix ◽  
Serum Free ◽  
Human Factor Ix ◽  
Recombinant Human Factor Ix ◽  
Serum Free Suspension

Reduced bleeding events with subcutaneous administration of recombinant human factor IX in immune-tolerant hemophilia B dogs

Blood ◽  
2003 ◽  
Vol 102 (13) ◽  
pp. 4393-4398 ◽  
Author(s):  
Karen E. Russell ◽  
Eva H. N. Olsen ◽  
Robin A. Raymer ◽  
Elizabeth P. Merricks ◽  
Dwight A. Bellinger ◽  
...  
Keyword(s):  
Human Factor ◽  
Subcutaneous Administration ◽  
Chronic Administration ◽  
Factor Ix ◽  
Hemophilia B ◽  
Enzyme Linked Immunosorbent Assay ◽  
Bleeding Events ◽  
Human Factor Ix ◽  
Immune Tolerant ◽  
Recombinant Human Factor Ix

AbstractIntravenous administration of recombinant human factor IX (rhFIX) acutely corrects the coagulopathy in hemophilia B dogs. To date, 20 of 20 dogs developed inhibitory antibodies to the xenoprotein, making it impossible to determine if new human FIX products, formulations, or methods of chronic administration can reduce bleeding frequency. Our goal was to determine whether hemophilia B dogs rendered tolerant to rhFIX would have reduced bleeding episodes while on sustained prophylactic rhFIX administered subcutaneously. Reproducible methods were developed for inducing tolerance to rhFIX in this strain of hemophilia B dogs, resulting in a significant reduction in the development of inhibitors relative to historical controls (5 of 12 versus 20 or 20, P < .001). The 7 of 12 tolerized hemophilia B dogs exhibited shortened whole blood clotting times (WBCTs), sustained detectable FIX antigen, undetectable Bethesda inhibitors, transient or no detectable antihuman FIX antibody titers by enzyme-linked immunosorbent assay (ELISA), and normal clearance of infused rhFIX. Tolerized hemophilia B dogs had 69% reduction in bleeding frequency in year 1 compared with nontolerized hemophilia B dogs (P = .0007). If proven safe in human clinical trials, subcutaneous rhFIX may provide an alternate approach to prophylactic therapy in selected patients with hemophilia B. (Blood. 2003;102:4393-4398)

scholarly journals Investigations into, and development of, a lyophilized and formulated recombinant human factor IX produced from CHO cells

2017 ◽  
Vol 39 (8) ◽  
pp. 1109-1120 ◽  
Author(s):  
Aline G. Almeida ◽  
Rodrigo C. V. Pinto ◽  
C. Mark Smales ◽  
Leda R. Castilho
Keyword(s):  
Cho Cells ◽  
Human Factor ◽  
Factor Ix ◽  
Human Factor Ix ◽  
Recombinant Human Factor Ix

scholarly journals Recombinant Human Factor IX Produced from Transgenic Porcine Milk

2014 ◽  
Vol 2014 ◽  
pp. 1-8 ◽  
Author(s):  
Meng-Hwan Lee ◽  
Yin-Shen Lin ◽  
Ching-Fu Tu ◽  
Chon-Ho Yen
Keyword(s):  
Human Factor ◽  
Specific Activity ◽  
Active Form ◽  
High Specific Activity ◽  
Factor Ix ◽  
Scale Production ◽  
Sialic Acid Content ◽  
Human Factor Ix ◽  
Recombinant Human Factor Ix ◽  
Porcine Milk

Production of biopharmaceuticals from transgenic animal milk is a cost-effective method for highly complex proteins that cannot be efficiently produced using conventional systems such as microorganisms or animal cells. Yields of recombinant human factor IX (rhFIX) produced from transgenic porcine milk under the control of the bovineα-lactalbumin promoter reached 0.25 mg/mL. The rhFIX protein was purified from transgenic porcine milk using a three-column purification scheme after a precipitation step to remove casein. The purified protein had high specific activity and a low ratio of the active form (FIXa). The purified rhFIX had 11.9γ-carboxyglutamic acid (Gla) residues/mol protein, which approached full occupancy of the 12 potential sites in the Gla domain. The rhFIX was shown to have a higher isoelectric point and lower sialic acid content than plasma-derived FIX (pdFIX). The rhFIX had the sameN-glycosylation sites and phosphorylation sites as pdFIX, but had a higher specific activity. These results suggest that rhFIX produced from porcine milk is physiologically active and they support the use of transgenic animals as bioreactors for industrial scale production in milk.

Production of recombinant human factor IX by propeptide modification in Drosophila S2 cell line

2019 ◽  
Vol 41 (3) ◽  
pp. 347-355
Author(s):  
Samira Bahrami ◽  
Mahmoud Ghaffari ◽  
Alireza Zomorodipour
Keyword(s):  
Cell Line ◽  
Human Factor ◽  
Factor Ix ◽  
Human Factor Ix ◽  
Recombinant Human Factor Ix
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