Sequencing of peptides and proteins with blocked N-terminal amino acids: N-acetylserine or N-acetylthreonine.

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Abstract
Many proteins cannot be directly sequenced by Edman degradation because they have a blocked N-terminal residue. A method is presented for deblocking such proteins when the N-terminal residue is N-acetylserine (which occurs frequently in eukaryotic proteins) or N-acetylthreonine. The method has been applied successfully to the determination of the N-terminal amino acid sequence of human, bovine, and rat parathymosins. Prothymosin .alpha. and other blocked proteins and peptides were also readily deblocked and sequenced by this procedure. It is proposed that the mechanism of the deblocking reaction involves an acid-catalyzed N .fwdarw. O shift of the acetyl group followed by a .beta.-elimination.