Purification of human erythropoietin

Human erythropoietin, derived from urine of patients with aplastic anemia, has been purified to apparent homogeneity. The seven-step procedure, which included ion exchange chromatography, ethanol precipitation, gel filtration, and adsorption chromatography, yielded a preparation with a potency of 70...

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Bibliographic Details
Published in:The Journal of biological chemistry 1977-08, Vol.252 (15), p.5558-5564
Main Authors: Miyake, T, Kung, C K, Goldwasser, E
Format: Article
Language:English
Subjects:
Anemia, Aplastic - urine
Electrophoresis, Polyacrylamide Gel
Erythropoietin - isolation & purification
Erythropoietin - urine
Humans
Hydrogen-Ion Concentration
Molecular Weight
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Summary:Human erythropoietin, derived from urine of patients with aplastic anemia, has been purified to apparent homogeneity. The seven-step procedure, which included ion exchange chromatography, ethanol precipitation, gel filtration, and adsorption chromatography, yielded a preparation with a potency of 70,400 units/mg of protein in 21% yield. This represents a purification factor of 930. The purified hormone has a single electrophoretic component in polyacrylamide gels at pH 9, in the presence of sodium dodecylsulfate at pH 7, and in the presence of Triton X-100 at pH 6. Two fractions of the same potency and molecular size, by sodium dodecyl sulfate gel electrophoresis, but differing slightly in mobility at pH 9, were obtained at the last step of fractionation. The nature of the difference between these two components is not yet understood.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)63387-9