This study describes the development of a universal phosphorylated peptide-binding protein designed to simultaneously detect serine,threonine and tyrosine kinases.The Escherichia coli alkaline phosphatase(EAP)is a wel...This study describes the development of a universal phosphorylated peptide-binding protein designed to simultaneously detect serine,threonine and tyrosine kinases.The Escherichia coli alkaline phosphatase(EAP)is a well-defined nonspecific phosphated monoesterase and Ser-,Thr-or Tyr-phosphorylated peptides served as substrates for EAP in preliminary experiments.Based on the known catalytic mechanism of EAP,the recombinant site-directed mutant EAP-S102L was generated,whose catalytic activity was blocked.展开更多
文摘This study describes the development of a universal phosphorylated peptide-binding protein designed to simultaneously detect serine,threonine and tyrosine kinases.The Escherichia coli alkaline phosphatase(EAP)is a well-defined nonspecific phosphated monoesterase and Ser-,Thr-or Tyr-phosphorylated peptides served as substrates for EAP in preliminary experiments.Based on the known catalytic mechanism of EAP,the recombinant site-directed mutant EAP-S102L was generated,whose catalytic activity was blocked.
