Human phosphoserine 31 corticotropin1-39. Isolation and characterization.
Two distinct forms of corticotropin1-39 (ACTH) were isolated and purified from an extract of three adult human pituitaries by reversed-phase chromatographic techniques. Structural studies indicated that the more polar form of ACTH was phosphorylated at serine residue 31. Approximately 30% of the ACTH was found in the phosphorylated form. A similar proportion of phosphorylated ACTH was observed in extracts of three pituitaries from human fetuses of 15, 17, and 20 weeks gestation. Phosphorylated and nonphosphorylated human ACTH1-39 were found to be steroidogenically equipotent using both an isolated rat adrenal cell bioassay and a cultured human fetal adrenal cell bioassay.
D000324:Adrenocorticotropic Hormone / Q000302:isolation & purification*; D000328:Adult; D000596:Amino Acids / Q000032:analysis; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D010446:Peptide Fragments / Q000032:analysis; D010768:Phosphoserine / Q000032:analysis*; D010902:Pituitary Gland / Q000032:analysis*; D012694:Serine / Q000031:analogs & derivatives*; D014357:Trypsin
D000596:Amino Acids; D010446:Peptide Fragments; D010768:Phosphoserine; D012694:Serine; D000324:Adrenocorticotropic Hormone; D014357:Trypsin