Application of chemical selective cleavage methods to analyze post-translational modification in proteins

✍ Scribed by Akira Tsugita; Kenji Miyazaki; Takuji Nabetani; Takehiro Nozawa; Masaharu Kamo; Takao Kawakami

• Publisher: John Wiley and Sons
• Year: 2001
• Tongue: English
• Weight: 141 KB
• Volume: 1
• Category: Article
• ISSN: 1615-9853
• DOI: 10.1002/1615-9861(200109)1:9<1082::aid-prot1082>3.0.co;2-u

✦ Synopsis

Application of chemical selective cleavage methods to analyze post-translational modification in proteins

Three chemical specific cleavage reactions, one for the carboxyl side of aspartyl peptide bonds, one for the carboxyl side of asparaginyl peptide bonds and another for the amino side of seryl/threonyl peptide bonds have been recently established. Additionally, these reactions simultaneously react on several post-translationally modified groups in peptides or proteins. The modified groups cover the external modifications N-formyl, N-acetyl, N-pyroglutamyi residues and C-terminal-a amide, as well as the internal modifications such as O-acetyl serine, phosphorylated serine/tyrosine, sulfonylated tyrosine, glycosylated serine/threonine and glycosylated asparagine. These three cleavage reactions relate to key amino acids for modifications, deamidation for asparagine, phosphorylation and acetylation for serine, and glycosylation for asparagine, serine and threonine. The chemical reactions on these modifications change the peptide mapping pattern, and information from these reactions may contribute characterization and location of post-translational modified groups in the protein.