The formation of dehydroalanine residues in alkali-treated insulin and oxidized glutathione. A nuclear-magnetic-resonance study

1H- and 13C-n.m.r. measurements enable direct observation of the rate of formation of dehydroalanine residues resulting from lysis of the disulphide bonds of insulin and oxidized glutathione in base at pD13. The data provide clear evidence for the beta-elimination mechanism for this reaction. The dehydroalanine-containing products from the lysis of insulin undergo secondary reactions.