Asparagine peptide was selectively cleaved by the Hofmann rearrangement followed by an alkaline treatment at the peptide linkage in which an amino group of the asparagine residue participated. Upon reaction of N-benzyloxycarbonyl-L-alanyl-L-asparagine with one equivalent of bromine and three equivalents of aqueous sodium hydroxide solution at 60° C, 1-(N-benzyloxycarbonyl-L-alanyl)-2-oxoimidazolidine-5-carboxylic acid was obtained in ...
