@article{3005079, title = "A radioimmunoassay for parathymosin α using antibodies to synthetic N-terminal peptide 1-30", author = "Tsitsiloni, O.E. and Yialouris, P.P. and Heimer, E.P. and Felix, A.M. and Evangelatos, G.P. and Soteriadis-Vlahos, C. and Stiakakis, J. and Hannappel, E. and Haritos, A.A.", journal = "Journal of Immunological Methods", year = "1988", volume = "113", number = "2", pages = "175-184", issn = "0022-1759", doi = "10.1016/0022-1759(88)90330-4", keywords = "epitope; radioisotope; synthetic peptide; thymosin, animal cell; animal experiment; cattle; cell culture; human; human cell; methodology; nonhuman; priority journal; rabbit; radioimmunoassay; rat, Adult; Aged; Amino Acid Sequence; Animal; Cattle; Chromatography, High Pressure Liquid; Cross Reactions; Female; Human; Immune Sera; Infant; Molecular Sequence Data; Peptide Fragments; Peptide Hydrolases; Rabbits; Radioimmunoassay; Support, Non-U.S. Gov't; Thymosin; Tissue Distribution", abstract = "Antibodies against the N-terminus of rat parathymosin α have been raised in rabbits by conjugating parathymosin α (1-30) to hemocyanin. A radioimmunoassay for parathymosin α was established by utilizing antibodies against the above polypeptide and parathymosin α(1-12)[Tyr] as tracer. The useful range was 5-450 pmol for parathymosin α. An epitope was located in the amino acid sequence 1-12. The antiserum failed to crossreact with the same molar concentrations of the partly homologous thymosin α1 or prothymosin α. With this radioimmunoassay, parathymosin α was isolated from calf thymus after separation from prothymosin α by reversed phase HPLC. Endogenous proteases did not appear to generate N-terminal fragments of parathymosin α in rat liver extracts in a similar fashion to that observed for prothymosin α. Parathymosin α has a ubiquitous distribution in the human tissues examined, with levels ranging from 93 (brain) to 1043 (liver) ng of parathymosin α(1-30) equivalents/g (wet weight). © 1988." }