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자료유형
학술저널
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한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제14권 제1호
발행연도
2004.1
수록면
140 - 147 (8page)

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Urokinase is an enzyme with fibrinolytic activity(plasminogen activator) isolated from fresh urine of healthymen. Viral safety is an important prerequisite for clinicalpreparation of the protein from urine. In order to increase theviral safety of a high purity urokinase in regard to nonenvelopedviruses, a virus removal process using a novelpolyvinylidene fluoride membrane filter (Viresolve NFP) hasbeen optimized. Urokinase was able to pass through the filterwith recoveries of 95% in the production scale process. Nosubstantial changes were observed in physical and biochemicalcharacteristics of the filtered urokinase in comparison withthose of the enzyme before filtration. A 47-mm disk membranefilter was used to simulate the process performance of theproduction scale cartridges and tested if it could removeseveral experimental model viruses for human pathogenicviruses, including porcine parvovirus (PPV), human hepatitisA virus (HAV), murine encephalomyocarditis virus (EMCV),bovine viral diarrhoea virus (BVDV), and bovine herpes virus(BHV). Non-enveloped viruses (PPV, HAV, and EMCV) aswell as enveloped viruses (BVDV and BHV) were completelyremoved during filtration. The log reduction factors achievedwere ³4.86 for PPV, ³4.60 for HAV, ³6.87 for EMCV, ³4.60for BVDV, and ³5.44 for BHV. These results indicate that thevirus filtration process successfully improved the viral safetyof the final products.

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