Identification of Formaldehyde-induced modifications in Diphtheria Toxoid

摘要

By combining accurate mass, the number of formaldehydeglycine modifications and CID, multistage and ETD fragmentation spectra, 85% of the mass spectral doublets were identified. Modified peptides derived from the catalytic domain and the receptor domain were found. Probably modifications in these functional sites contribute to the detoxification of the diphtheria toxin.