Isolation of two biologically active peptides, erythrotropin I and erythrotropin II from fetal calf intestine.
A bioassay based on the measurement of thymidine incorporation into trichloroacetic acid-insoluble materials in erythroid cell suspensions from fetal calf liver was used as the assay for purification of two small peptides (erythrotropins I and II) from fetal calf intestine. The peptides were purified using reversed-phase and gel permeation high performance liquid chromatography (HPLC). The two peptides have very similar amino acid compositions and a molecular weight of about 3500 daltons. Erythrotropin II stimulated thymidine incorporation and potentiated the action of erythropoietin in cultures of erythroid cells from fetal rat liver.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001681:Biological Assay; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D004900:Erythroblasts / Q000187:drug effects / Q000378:metabolism; D005260:Female; D036341:Intercellular Signaling Peptides and Proteins; D007422:Intestines / Q000032:analysis / Q000196:embryology*; D008970:Molecular Weight; D010455:Peptides / Q000302:isolation & purification*; D011247:Pregnancy; D013936:Thymidine / Q000378:metabolism
D000596:Amino Acids; D036341:Intercellular Signaling Peptides and Proteins; D010455:Peptides; C039299:erythrotropin; D013936:Thymidine