Identification and Characterization of O-Biotinylated Hydroxy Amino Acid Residues in Peptides

B. T. Miller, M. E. Rogers, J. S. Smith, A. Kurosky

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    17 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

    • Molecular Biology
    • Biophysics
    • Biochemistry

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