The hormone erythropoietin (EPO), released under hypoxic conditions, acts primarily to stimulate erythrocyte (RBC) production. The association between lack of oxygen, a blood-borne compound, and RBC formation was suggested as early as at the turn of the century (Carnot & DeFlandre, 1906), but it was not until 1957 that the kidneys were identified as the major site of EPO production in the adult mammal (Jacobson et al. 1957). The first purification of EPO was from plasma of anaemic sheep in 1971 (Goldwasser & Kung, 1971). Despite an extensive procedure, the yield and specific activity of the product were extremely low (0·4% and 8250 U/mg protein respectively). In 1977, the same procedure was used with 2550 litres of urine from anaemic humans, generating a product with a specific activity of 74 000 U/mg protein (Miyake et al. 1977). Characterization of the hormone was hampered by the difficulty of obtaining a
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