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• W2166531101 abstract "A rapid and simple chromatographic procedure has been developed for the large‐scale purification of therapeutic‐grade rHuEPO (recombinant human erythropoietin) from medium‐conditioned cell cultures, which includes ion‐exchange, hydrophobic‐interaction and gel‐filtration chromatography. A combination of these well‐connected steps results in highly purified rHuEPO (>99%), as revealed by SDS/PAGE and HPLC analyses, with a total yield of 38%. The specific activity of purified rHuEPO was 160104 i.u./mg. Immunoblotting studies revealed that the protein possesses native EPO immunity. N‐terminal sequencing of rHuEPO shows that the first 15 amino acids coincide with those of native EPO reported previously." @default.
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• W2166531101 date "2004-08-01" @default.
• W2166531101 modified "2023-10-14" @default.
• W2166531101 title "An improved, inexpensive procedure for the large-scale purification of recombinant human erythropoietin" @default.
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• W2166531101 doi "https://doi.org/10.1042/ba20030189" @default.
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