CLEAVAGE OF DEHYDROALANINE‐CONTAINING PEPTIDES WITH MERCURIC ACETATE

Abstract
The dehydroalanine containing peptides glycyldehydroalanine and t-butyloxycarbonyl-L-alanyldehydroalanyl-β-methyl-D,L-aspartic acid methyl ester were synthesized, respectively, from chloroacetamide and pyruvate and from t-butyloxycarbonyl-L-alanyl-S-methyl-L-cysteinyl-β-methyl-D,L -aspartic acid methyl ester. They were reacted with mercuric acetate in water, 50% methanol and dimethylformamide at 25° and at 80° for various time periods. Reaction proceeded to yield an amino acid amide from the N-terminal side of the unsaturated residue and pyruvate from the C-terminal side. Yields of amino acid amides were 76% for the dipeptide and 40% for the tripeptide. The applicability of the neutral reaction conditions employed to the cleavage of glycoproteins containing both O- and N-glycosidically-linked carbohydrate chains following β- elimination of the serine and threonine linked oligosaccharides is pointed out.

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