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Cited by 886

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Purification of human erythropoietin.

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Miyake, T, Kung, C K, Goldwasser, E·1977·Journal of Biological Chemistry

Abstract

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.

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Metadata

Authors
Miyake, T., Kung, C. K., & Goldwasser, E.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1977-08
Volume
252
Issue
15
Pages
5558-5564
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1541049769
Cited by
886
References
0
FWCI
11.46
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Purification of human erythropoietin. https://app.cochat.ai/papers/10.1016/s0021-9258(19)63387-9
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Miyake, T., Kung, C. K., & Goldwasser, E. (1977). Purification of human erythropoietin. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)63387-9

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.