Dynorphin A(1-8) in human placenta: Amino acid sequence determined by tandem mass spectrometry

Abdulbaki Agbas, Mahmoud S. Ahmed, William Millington, Bojana Cemerikic, Dominic M. Desiderio, Jih Lie Tseng, Chhabil Dass

Research output: Contribution to journalArticle

8 Scopus citations

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 languageEnglish (US)
Pages (from-to)623-627
Number of pages5
JournalPeptides
Volume16
Issue number4
DOIs
StatePublished - 1995
Externally publishedYes

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Keywords

  • Amino acid sequence
  • Dynorphin A(1-8)
  • Human placenta

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience

Cite this

Agbas, A., Ahmed, M. S., Millington, W., Cemerikic, B., Desiderio, D. M., Tseng, J. L., & Dass, C. (1995). Dynorphin A(1-8) in human placenta: Amino acid sequence determined by tandem mass spectrometry. Peptides, 16(4), 623-627. https://doi.org/10.1016/0196-9781(95)00013-A