Open AccessMass spectrometric charting of bovine posterior/intermediate pituitary peptides.
Author(s) -
Gottfried J. Feistner,
Peter Højrup,
Christopher J. Evans,
Douglas F. Barofsky,
Kym F. Faull,
Peter Roepstorff
Publication year - 1989
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.86.16.6013
Subject(s) - proopiomelanocortin , glycopeptide , peptide , chemistry , posterior pituitary , molecular mass , peptide sequence , biochemistry , pituitary gland , fast atom bombardment , computational biology , biology , chromatography , mass spectrometry , gene , enzyme , hormone , antibiotics
The feasibility for charting neuropeptides in neuroendocrine tissues on the basis of the universal property and inherent specificity of their molecular weights was explored. As a model, a comprehensive MS analysis of extractable peptides from bovine posterior/intermediate pituitary was performed. Two suitable MS techniques--namely, plasma-desorption time-of-flight and fast atom bombardment MS--were evaluated, and each method could identify more than 20 peptides, including N-terminally acetylated and C-terminally amidated species. In toto these peptides account for almost the entire lengths of propressophysin, prooxyphysin, and proopiomelanocortin. Some of the experimentally determined molecular weights did not match any known peptides. Three of these species were identified as acidic joining peptide (4-24) [proopiomelanocortin(83-103)], C-terminal glycopeptide(22-39) [propressophysin(130-147)], and glycosylated C-terminal glycopeptide(1-19) [propressophysin(109-127)] by conventional sequence analysis.