Abstract
Presence of the kappa receptor-preferring neuropeptide dynorphin A(1-8) in human placenta has been demonstrated by mass spectrometry to establish rigorously the appropriate molecular weight and amino acid sequence. Liquid secondary ionization mass spectrometry produced the protonated molecule ion, (M + H)+, at m/z 981 of the endogenous peptide, and tandem mass spectrometry collected the product ion spectrum that contained the appropriate amino acid sequence-determining fragment ions produced from the precursor ion (M + H)+. The amino acid sequence of the peptide is YGGFLRRI.
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