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A Chemically Designed Enzymatic Cleavage Site for Phosphoproteome Analysis
Author(s) -
Peng Jianhe
Publication year - 2004
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200400016
Subject(s) - threonine , lysine , cleavage (geology) , serine , chemistry , enzyme , phosphorylation , biochemistry , phosphopeptide , amino acid , biology , paleontology , fracture (geology)
Targeting phosphorylated serine and threonine enzymatically. pS and pT have been chemically modified into lysine homologues that are sensitive to a lysine‐specific enzyme. The existence of phosphorylated residues could be inferred from the presence of the cleavage sites. Moreover, it has been demonstrated that this approach is practical for the enrichment of pS‐ and pT‐containing peptides. This is a big contribution to phosphoproteome analysis.