A new method was developed for determination of disulfide pairings in peptides. This method consisted in the synthesis of peptides with deuteriocysteine residues at given positions and the analysis of deuteriocystine generated in the acid hydrolyzates of the synthetic peptides by fast atom bombardment mass spectrometry. The availability of this method was confirmed by its application for determining the positions of disulfide linkages in a heat-stable enterotoxin of enterotoxigenic Escherichia coli.
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Hidaka et al. (1989) studied this question.
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