THE NEW METHOD OF PURIFICATION FACTOR COAGULATION VIII
(Abstract release date: 05/18/17)
EHA Library. Shurko N. 05/18/17; 182951; PB2238
Dr. Nataliya Shurko
Contributions
Contributions
Abstract
Abstract: PB2238
Type: Publication Only
Background
The human plasma of blood can be transfused directly to patients or pooled and fractionated into plasma protein products. Plasma contains about 60-80 g/L of protein, of which about 95 % are used for many therapeutic products. The main proteins that use for treatment many diseases are albumine (45 g/L), immunoglobulin (8-11 g/L), factors coagulations. The Factor VIII (FVIII) is one of the blood coagulation factor and it deficient causing development of bleeding desorders known as Haemophilia A. The purification of FVIII is generally required for the treatment Haemophilia A or von Willebrand’s disease and heavy loss of blood, requires relatively high purity for medical use.
Aims
optimization of a process purification of FVIII by the method of affinity chromatography on the Diasorb-aminopropyl matrix with triazin active dyes as ligands.
Methods
adsorption/precipitation, ion-exchange chromatography on DEAE-Sepharose, affinity chromatography on the Diasorb-aminopropyl matrix with Active Scarlet Damask 4GT as ligands in combination methods of antiviral treatment.
Results
The process plasma fractionation is largest industry segment in manufacture of therapeutic concentrate of plasma proteins. We developed technological scheme that involves fractionation plasma of blood in combinations of classical methods of protein precipitation and two chromatographic steps: ion exchange and affinity chromatography.
Of all plasma fractionation methods, chromatography is the best candidate for purification of factor coagulation, especially FVIII. The methods adsorption/precipitation permits the fractionation of large volumes of plasma, but the quality of the product obtained by chromatography is superior.
We offer: fresh frozen plasma – adsorption of proteins on the barium citrate – adsorption of proteins on Al(OH)3 – adsorption of proteins to PEG-4000 – viral inactivation (solvent-detergent method) – ion exchange chromatography on DEAE-Sepharose – viral inactivation (ammonium thiocyanate) – dye-ligand affinity chromatography (Diasoorb-Active Scarlet Damask 4GT). We got the drug of FVIII with specific activity 69.65 ± 2.24 IU/mg protein.
Conclusion
we developed technological scheme of plasma fractionation and reached a high degree of purification of coagulation FVIII.
Session topic: 30. Transfusion medicine
Keyword(s): transfusion, Hemophilia A, Coagulation Factor VIII
Abstract: PB2238
Type: Publication Only
Background
The human plasma of blood can be transfused directly to patients or pooled and fractionated into plasma protein products. Plasma contains about 60-80 g/L of protein, of which about 95 % are used for many therapeutic products. The main proteins that use for treatment many diseases are albumine (45 g/L), immunoglobulin (8-11 g/L), factors coagulations. The Factor VIII (FVIII) is one of the blood coagulation factor and it deficient causing development of bleeding desorders known as Haemophilia A. The purification of FVIII is generally required for the treatment Haemophilia A or von Willebrand’s disease and heavy loss of blood, requires relatively high purity for medical use.
Aims
optimization of a process purification of FVIII by the method of affinity chromatography on the Diasorb-aminopropyl matrix with triazin active dyes as ligands.
Methods
adsorption/precipitation, ion-exchange chromatography on DEAE-Sepharose, affinity chromatography on the Diasorb-aminopropyl matrix with Active Scarlet Damask 4GT as ligands in combination methods of antiviral treatment.
Results
The process plasma fractionation is largest industry segment in manufacture of therapeutic concentrate of plasma proteins. We developed technological scheme that involves fractionation plasma of blood in combinations of classical methods of protein precipitation and two chromatographic steps: ion exchange and affinity chromatography.
Of all plasma fractionation methods, chromatography is the best candidate for purification of factor coagulation, especially FVIII. The methods adsorption/precipitation permits the fractionation of large volumes of plasma, but the quality of the product obtained by chromatography is superior.
We offer: fresh frozen plasma – adsorption of proteins on the barium citrate – adsorption of proteins on Al(OH)3 – adsorption of proteins to PEG-4000 – viral inactivation (solvent-detergent method) – ion exchange chromatography on DEAE-Sepharose – viral inactivation (ammonium thiocyanate) – dye-ligand affinity chromatography (Diasoorb-Active Scarlet Damask 4GT). We got the drug of FVIII with specific activity 69.65 ± 2.24 IU/mg protein.
Conclusion
we developed technological scheme of plasma fractionation and reached a high degree of purification of coagulation FVIII.
Session topic: 30. Transfusion medicine
Keyword(s): transfusion, Hemophilia A, Coagulation Factor VIII
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