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초록
영어
The human albumin has long half-life and good stability, so it could be a candidate for component to increase half-life and efficacy of therapeutic proteins1). Half-life of erythropoietin(EPO) is necessary to enhance the stability in vivo. We designed the human albumin fused N-terminal of EPO and inserted linker between albumin and EPO2). In vivo half-life of recombinant
human albumin-EPO fusion protein (rhAlbumin-EPO) was evaluated in femoral vein-cannulated SD-Rat (4ug EPO/kg). Blood samples were obtained from orbital sinus and EPO was quantified by ELISA. Efficacy of rhAlbumin-EPO was compared with standard EPO (BRP) using normothaemic mice (B6D2F1) at the dose of 20, 40 and 80 IU per individual subcutaneously.
Amounts of reticulocytes were counted by CultersⓇ FACS analyzer at each dose. As the results, half-life of rhAlbumin-EPO was increased 2.5-fold and efficacy was 64-fold higher than standard EPO.