Abstract

The difficulties presented by sulfur-containing amino acids in mass spectrometric sequencing of peptides can be eliminated by reductive desulfuration in the presence of an easily prepared and efficient Ni 2B catalyst. The procedure described consisting of reductive desulfuration, isobutoxycarbonylation and permethylation allows simple and rapid modification of small levels of peptides, and advances the potential of mass spectrometry as a tool in peptide sequencing procedures.

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