title: Characterization of purified human erythroid-potentiating activity.
abstract: Erythroid-potentiating activity (EPA), purified from serum-free medium conditioned by the Mo human T-lymphoblast cell line, is a 28,000 dalton glycoprotein. Removal of carbohydrate from EPA by digestion with endoglycosidase F generates a protein with an apparent molecular weight of 18,000. We have used purified EPA to develop rabbit antisera which neutralize the burst-promoting activity of purified EPA. These antisera immunoprecipitate a 28,000-dalton glycoprotein from metabolically labeled Mo cells. Purified EPA stimulates murine and human BFU-E and CFU-E but not myeloid or macrophage colonies.
mesh_terms: D000818:Animals; D002460:Cell Line; D002478:Cells, Cultured; D011232:Chemical Precipitation; D004920:Erythropoiesis; D006026:Glycoside Hydrolases; D006412:Hematopoietic Stem Cells / Q000502:physiology*; D006801:Humans; D008214:Lymphocytes / Q000378:metabolism; D008222:Lymphokines / Q000302:isolation & purification*; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D051379:Mice; D008970:Molecular Weight; D011863:Radioimmunoassay; D013045:Species Specificity; D019714:Tissue Inhibitor of Metalloproteinases
chemical_list: D008222:Lymphokines; D019714:Tissue Inhibitor of Metalloproteinases; D006026:Glycoside Hydrolases; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase