AbstractActivation of guanosine 3′,5′-cyclic monophosphate phosphodiesterase in outer-segment membrane of chicken retina was investigated. Irradiation of dark-adapted chicken outer segment membrane for bleaching of iodopsin increased the enzyme activity twice as much as that in the dark in the presence of GTP. Further irradiation of the sample for bleaching of rhodopsin in the membrane induced some additional activation of the enzyme. However, chicken iodopsin activated the enzyme in frog rod outer segment membrane without irradiation, while chicken rhodopsin did not. Irradiation of chicken iodopsin increased the enzyme activity twice as much as that in the dark
AbstractCNBr treatment of rod outer segments was performed in dark and in light conditions. With the...
AbstractTβγ was shown to stimulate the hydrolysis and synthesis of PtdInsP2 in dark-adapted bovine r...
AbstractIn vivo phosphorylation of Pγ, an inhibitory subunit of cGMP-phosphodiesterase of frog (Rana...
AbstractActivation of guanosine 3′,5′-cyclic monophosphate phosphodiesterase in outer-segment membra...
AbstractATP quenches light-dependent phosphodiesterase (PDE) activation in rod outer segments presum...
AbstractIodopsin (a red-sensitive cone visual pigment) and rhodopsin (a rod pigment) were isolated f...
AbstractActivation of cGMP phosphodiesterase(PDE) of frog rod outer segments (ROS) by purified green...
The hydrolysis of cyclic guanosine monophosphate (cyclic GMP) and of guanosine triphosphate (GTP) by...
AbstractA purified iodopsin was digested by CNBr or several proteolytic enzymes into fragments, the ...
Light activates rod outer segment (ROS) phosphodiesterase (PDEase), as shown by previous biochemical...
AbstractThe effects of a 26 kDa protein isolated from vertebrate retina rod outer segments (ROS) and...
Journal ArticleA simple purification method has been developed for isolation of bovine cGMP phosphod...
AbstractPhotoreceptor outer segments isolated from squid retina are known to contain a light-activat...
AbstractThe so-called AT-signal described here is a transient light-induced increase of the near-inf...
Structural studies on photoreceptor phosphodiesterases type 6 (PDE6s) have been hampered by an inabi...
AbstractCNBr treatment of rod outer segments was performed in dark and in light conditions. With the...
AbstractTβγ was shown to stimulate the hydrolysis and synthesis of PtdInsP2 in dark-adapted bovine r...
AbstractIn vivo phosphorylation of Pγ, an inhibitory subunit of cGMP-phosphodiesterase of frog (Rana...
AbstractActivation of guanosine 3′,5′-cyclic monophosphate phosphodiesterase in outer-segment membra...
AbstractATP quenches light-dependent phosphodiesterase (PDE) activation in rod outer segments presum...
AbstractIodopsin (a red-sensitive cone visual pigment) and rhodopsin (a rod pigment) were isolated f...
AbstractActivation of cGMP phosphodiesterase(PDE) of frog rod outer segments (ROS) by purified green...
The hydrolysis of cyclic guanosine monophosphate (cyclic GMP) and of guanosine triphosphate (GTP) by...
AbstractA purified iodopsin was digested by CNBr or several proteolytic enzymes into fragments, the ...
Light activates rod outer segment (ROS) phosphodiesterase (PDEase), as shown by previous biochemical...
AbstractThe effects of a 26 kDa protein isolated from vertebrate retina rod outer segments (ROS) and...
Journal ArticleA simple purification method has been developed for isolation of bovine cGMP phosphod...
AbstractPhotoreceptor outer segments isolated from squid retina are known to contain a light-activat...
AbstractThe so-called AT-signal described here is a transient light-induced increase of the near-inf...
Structural studies on photoreceptor phosphodiesterases type 6 (PDE6s) have been hampered by an inabi...
AbstractCNBr treatment of rod outer segments was performed in dark and in light conditions. With the...
AbstractTβγ was shown to stimulate the hydrolysis and synthesis of PtdInsP2 in dark-adapted bovine r...
AbstractIn vivo phosphorylation of Pγ, an inhibitory subunit of cGMP-phosphodiesterase of frog (Rana...