Electrochemical evaluation of self-disassociation of PKA upon activation by cAMP.
The allosteric reaction of protein kinase A (PKA) upon binding of cyclic AMP (cAMP) is revealed with an electrochemical technique through the redox current change of an electrochemically active marker. The different effect of cAMP's regulation at a distinct concentration level is obtained in this system. The influence of structural analogues is also examined with respect to the affinity and special selectivity. This study presents an electrochemical approach to the rapid and sensitive investigation of the protein-ligand interaction in the signal transduction networks.
Xiao
Han
H
Department of Biochemistry and National Key Laboratory of Pharmaceutical Biotechnology, Nanjing University, Nanjing 210093, PR China.
Wang
Jing
J
Chen
Guifang
G
Li
Genxi
G
D000818:Animals; D002417:Cattle; D000242:Cyclic AMP / Q000737:chemistry*; D017868:Cyclic AMP-Dependent Protein Kinases / Q000737:chemistry*; D004563:Electrochemistry; D004789:Enzyme Activation; D008024:Ligands; D015398:Signal Transduction
D008024:Ligands; D000242:Cyclic AMP; D017868:Cyclic AMP-Dependent Protein Kinases