Mass spectrometric signature of S-prenylated cysteine peptides

Anal Biochem. 1991 Mar 2;193(2):173-7. doi: 10.1016/0003-2697(91)90004-d.

Abstract

The fast atom bombardment mass spectra of peptides containing S-prenylated cysteine display signature fragmentations characteristic of this modified amino acid. The fragmentation is independent of the nature of the cysteine carbonyl substituent, easily differentiates prenyl from nonprenyl alkylation, and readily identifies the oligomer count of the prenyl. This screening method, which requires little time, effort, or material (compared with previous analysis methods based on chemical degradation), greatly facilitates the identification of these prenylated proteins.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Cysteine / chemistry*
  • Mating Factor
  • Molecular Sequence Data
  • Oligopeptides / chemistry*
  • Peptide Fragments / chemistry*
  • Peptides / chemistry*
  • Protein Processing, Post-Translational
  • Spectrometry, Mass, Fast Atom Bombardment

Substances

  • Oligopeptides
  • Peptide Fragments
  • Peptides
  • Mating Factor
  • Cysteine