Identification and characterization of o-biotinylated hydroxy amino acid residues in Peptides

Brian T. Miller, Mark E. Rogers, John S. Smith, Alexander Kurosky

Research output: Contribution to journalArticle

17 Scopus citations

Abstract

Recent findings have indicated that certain hydroxyl groups of peptides have enhanced intrinsic chemical reactivity and can be O-acylated by N-hydroxysuccinimide esters of biotin. Analytical procedures are described for the identification of O-acylated derivatives of seryl, threonyl, and tyrosyl residues after reaction with the N-hydroxysuccinimide ester of biotin containing the extended spacer arm 6-aminohexanoic acid. The identification and chemical characterization of O-biotinylated residues included amino acid analysis, peptide sequence determination, and mass spectrometric analysis. The application of these analytical procedures provided unequivocal identification of O-biotinylated residues for a number of peptides investigated. In a separate study, we also show that O-biotinylated amino-terminal seryl residues occurring after proteolysis of peptides or proteins can rapidly undergo an O → N acyl shift resulting in blockage of sequence analysis by the Edman degradation procedure.

Original languageEnglish (US)
Pages (from-to)240-248
Number of pages9
JournalAnalytical Biochemistry
Volume219
Issue number2
DOIs
StatePublished - Jun 1994

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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