Premium
Erythropoiesis Stimulating Factors
Author(s) -
Lewis Jasper P.,
Alford Dorothy A.,
Neal W. Aubrey,
Moores Russel R.,
Welch Emily T.,
Gardner Edward,
Wright ClaudeStarr,
Smith Linda L.
Publication year - 1971
Publication title -
scandinavian journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.904
H-Index - 84
eISSN - 1600-0609
pISSN - 0036-553X
DOI - 10.1111/j.1600-0609.1971.tb01974.x
Subject(s) - fucose , erythropoiesis , chemistry , glycoprotein , sialic acid , erythropoietin , steroid , hormone , ultrafiltration (renal) , biochemistry , chromatography , endocrinology , medicine , biology , anemia
A urine concentrate of erythropoietin, obtained by chromatography on diethylamino‐ethyl (DEAE)‐cellulose, contained regulators of erythropoiesis that could be fractionated by selective membrane permeability. Two erythropoiesis stimulating factors (ESF) were obtained after exhaustive dialysis, one that diffused through the membrane and one in the retentate. A biochemical study of the ESF in the diffusate showed no appreciable sialic acid or fucose, a trace of hexosamine and a relatively small amount of protein. The remainder of the complex appeared to be an adrenocorticosteroid(s). The protein appeared to be a fragment of a glycoprotein. After exhaustive dialysis the retentate‐ESF had the characteristics of an ESF‐generating factor. The optimum pH for activity was about 7.4. It is suggested that an ESF(s) remains inactive when bound to a glycoprotein such as α 1 ‐acid glycoprotein or the corticosteroid‐binding globulin. A role of an ESF‐generating factor would be to act on the complex to produce a fragment of the glycoprotein steroid complex, thereby activating the hormone.