• Record: found
  • Abstract: found
  • Article: not found

Chemical cleavage at aspartyl residues for protein identification.

Analytical Chemistry

Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Animals, Aspartic Acid, chemistry, Formates, Hydrolysis, Peptide Fragments, Peptide Mapping, methods, Proteins, Sequence Analysis, Protein

Read this article at

      There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.


      An alternative method to enzymatic digestion for protein identification by mass spectrometry has been developed that is based on chemical cleavage by formic acid. This method was tested on gel-purified apomyoglobin and BSA, as well as unknown proteins that cofractionate with Tyl-virus-like particles from Saccharomyces cerevisiae. Cleavage at aspartyl residues was found to be efficient and specific, and this specificity of cleavage lent itself easily to database searches. Parallel digestions using trypsin were also performed. The formic acid cleavage method generated comparable or better results than tryptic digestion for protein identification.

      Related collections

      Author and article information



      Comment on this article