preparation of highly purified solventdetergent coa gulation factor vii and factor ix concentrates from prothrombin complex (ppsb)

نویسندگان

s nasiri from the department of research and development, blood research and fractionation co., tehran, and the *department of virology, tarbiat modarres university, tehran, i.r. iran.

h rezvan

k mousavi

mh roostaei

چکیده

in this study, anion-exchange chromatography was used to purify factor vii and factor ix from prothrombin complex (ppsb), which contains coagulation factors ii, vii, ix and x. for this purpose, deae-sepharose cl-6b gel , pharmacia column xk-26 , high flow rate and two stepwise gradients with phosphate citrate buffer were used. the yield of the two lyophylized products, factor vii and factor ix concentrates, was 61 % and 75%, respectively. specific activity of factor vii increased from 0.16 to 3.06 (purification-fold= 19.1) and specific activity of factor ix increased from 12 to 4.9 (purification-fold= 4.1). results of electrophoresis on agarose gel-as well as immunoelectrophoresis-indicated higher purity of factor vii and factor ix compared to ppsb. thrombogenicity of the two products were within the normal range defined for ppsb. in order to improve viral safety, solvent-detergent treatment was performed prior to further purification. factor vii concentrate is used for patients with factor vii deficiency and also for hemophilia patients with inhibitors. factor ix concentrate is used for treatment of hemophilia b patients.

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عنوان ژورنال:
medical journal of islamic republic of iran

جلد ۱۵، شماره ۲، صفحات ۱۰۳-۱۰۸

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