Serial VCG/ECG Analysis Using Neural Networks

Transducin (T) mediates vision in retinal rods by transmitting light signals detected by rhodopsin to a cGMP phosphodiesterase. The flow of information relies on a subunit association/dissociation cycle of T regulated by a guanine nucleotide exchange/hydrolysis reaction. 5'-[p-(Fluorosulfonyl)benzoyl] guanosine (FSBG) was synthesized and examined here as an affinity label for the guanine nucleotide binding site of T. Although the relative binding affinity of FSBG to T was much lower than for GTP and beta,gamma-imido-guanosine 5'-triphosphate (GMPPNP), the incorporation of FSBG to T inhibited its light-dependent [(3)H] GMPPNP binding activity in a concentration dependent manner. Additionally, GDP, GTP and GTP analogs hindered the binding of [(3)H] FSBG to T. These results demonstrated that FSBG could be used to specifically modify the active site of T. In addition, FSBG was not capable of dissociating T from T:photoactivated rhodopsin complexes, suggesting that in this case FSBG is acting as a GDP analog.

show abstract

Serial VCG/ECG Analysis Using Neural Networks

Cited by 9 publications

References 13 publications

Computer Analysis of the Electrocardiogram

Computer Analysis of the Electrocardiogram

Computer Analysis of the Electrocardiogram

Use of 5′-[p-(Fluorosulfonyl)benzoyl] Guanosine as an Affinity Probe for the Guanine Nucleotide-Binding Site of Transducin

Contact Info

Product

Resources

About