J. Biol. Chem., Vol. 259, Issue 5, 2707-2710, Mar, 1984
Isolation of human erythropoietin with monoclonal antibodies
S Yanagawa, K Hirade, H Ohnota, R Sasaki, H Chiba, M Ueda and M Goto
Human erythropoietin was isolated from urine of aplastic anemic patients in
a high yield with a simple purification procedure using an immunoadsorbent
column of monoclonal antibodies and a Sephadex G-100 column. About 6 mg of
erythropoietin was isolated from 700 liters of urine and the specific
activity was estimated to be 81,600 units/mg of protein with an in vivo
59Fe incorporation assay method, using starved rats. Activity measurement
of the extracts from sliced gels after sodium dodecyl
sulfate-polyacrylamide gel electrophoresis and the Western blotting
technique revealed heterogeneity of the isolated erythropoietin, which is
probably caused by variable amounts of carbohydrates attached to the
polypeptide chain. Thirty amino acids in the NH2-terminal portion of the
isolated hormone were sequenced.
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