Abstract
When a polypeptide containing .gamma.-carboxyglutamic acid is decarboxylated in 2H2O, residue of (.gamma..gamma.-2H2)glutamic acid are formed. Subsequent proteolytic digestion produces peptides which contain at each site 2H2-substituted and unsubstituted glutamic acid in the same ratio as existed for .gamma.-carboxy-substitution. The peptides may be identified and this ratio determined by combined gas chromatography-mass spectrometry. Decarboxylation in 3H2O followed by amino-acid analysis and Edman degradation are also discussed.