T. Miyake led the byline of a 1977 report, with C. K. Kung and E. Goldwasser, describing purification of human erythropoietin. Ion-exchange chromatography, gel filtration and other separations yielded an active hormone preparation with -fold purification and activity recovery.[ref]
Purity and recovery measure different achievements. For a hypothetical starting sample with activity units, recovery leaves units even if most unwanted proteins have been removed. A high purification factor therefore does not mean that nearly all of the starting erythropoietin survived.

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