期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1990
卷号：87
期号：5
页码：1947-1949
DOI：10.1073/pnas.87.5.1947
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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----O shift of the acetyl group followed by a beta-elimination.
