Erythropoietin: isolation by affinity chromatography with lectin-agarose derivatives.

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Abstract
Affinity chromatography using agarose-bound lectins was used to isolate erythropoietin from crude preparations of sheep plasma and human urinary erythropoietin. Based on previous estimates of the sugar content of the hormone, 6 lectins (wheat germ agglutinin, phytohemagglutinin, Ricinus communis 120, soybean agglutinin, concanavalin A and [Limulus polyphemus] limulin) were chosen for study. Only wheat germ agglutinin-agarose and phytohemagglutinin-agarose derivatives had significant affinity for erythropoietin. By use of wheat germ agglutinin-agarose columns, erythropoietin could be separated from over 95% of the initial starting protein, resulting in a 8- to 100-fold purification and a recovery of at least 40% depending on the hormone source. Affinity chromatography with agarose-bound lectins provides a simple rapid method for isolating erythropoietin from crude preparations of the hormone.