Abstract
Presence of the κ 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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 623-627 |
| Number of pages | 5 |
| Journal | Peptides |
| Volume | 16 |
| Issue number | 4 |
| DOIs | |
| State | Published - 1995 |
| Externally published | Yes |
Keywords
- Amino acid sequence
- Dynorphin A(1-8)
- Human placenta
ASJC Scopus subject areas
- Biochemistry
- Physiology
- Endocrinology
- Cellular and Molecular Neuroscience