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 journalArticlepeer-review

    18 Scopus citations


    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
    Issue number2
    StatePublished - Jun 1994

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology
    • Cell Biology


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