Nature und Extent of Peptide Bond Cleavage by Anhydrous Heptafluorobutyric Acid during Edman Degradation

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Abstract
During the isothiocyanate degradation of proteins a gradual increase in the level of all thiohydantoin derivatives of amino acids occurs, which progressively obscures the sequential identification of the significant N-terminal amino acids. The major cause for this was a hitherto unknown specific cleavage at aspartic acid residues in anhydrous heptafluorobutyric acid and to a lesser extent, the N .fwdarw. O shift in peptide bonds involving hydroxyamino acids. Measures to reduce susceptibility of the peptide bonds at these sites are described.

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