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Detection and characterization of native β‐endorphin 1–31 in bovine pituitary using electrospray ionization, liquid secondary ion and tandem mass spectrometry
Author(s) -
Yan Lin,
Tseng JihLie,
Desiderio Dominic M.
Publication year - 1995
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/jms.1190300403
Subject(s) - chemistry , protein mass spectrometry , electrospray ionization , chromatography , tandem mass spectrometry , sample preparation in mass spectrometry , mass spectrometry , electrospray , trypsin , liquid chromatography–mass spectrometry , bottom up proteomics , top down proteomics , biochemistry , enzyme
The molecular ion of intact β‐endorphin bovine, 1–31 (BE), which was extracted from bovine pituitary, was determined by electrospray ionization mass spectrometry. Liquid secondary ion mass spectrometry determined the molecular masses of three peptides produced by trypsin digestion of BE, and tandem mass spectrometry was used to determine the amino acid sequence of the tryptic peptide BE 20–24 . These data, in combination, were used to characterize BE in bovine pituitary.