Erythropoietin: isolation by affinity chromatography with lectin-agarose derivatives

J. L. Spivak, D. Small, M. D. Hollenberg

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Affinity chromatography using agarose-bound lectins was used to isolate erythropoietin from crude preparations of sheep plasma and human urinary erythropoietin. On the basis of previous estimates of the sugar content of the hormone, six lectins (wheat germ agglutinin, phytohemagglutinin, Ricinus communis 120, soybean agglutinin, concanavalin A, and 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 an 8- to 100-fold purification and a recovery of at least 40% depending on the source of the hormone. Affinity chromatography with agarose-bound lectins provides a simple rapid method for isolating erythropoietin from crude preparations of the hormone.

Original languageEnglish (US)
Pages (from-to)4633-4635
Number of pages3
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number10
StatePublished - 1977

ASJC Scopus subject areas

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