[cGMP-binding centers in photoreceptor membranes].
The binding of cGMP by structural components of bovine rod outer segments was studied. The discs and plasma membranes were shown to contain two types of the specific binding sites for cGMP which are distinct from cyclic GMP phosphodiesterase. The sites have a "high" and "low" (Kd = 0.1 divided by 0.35 and 1.5 divided by 2.0 X 10(-6) M respectively) affinity for cGMP. They belong to membraneous integral proteins presumably associated with phospholipids. Their affinity for cGMP is controlled by GTP and calmodulin.
D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism; D002147:Calmodulin / Q000378:metabolism; D002417:Cattle; D002462:Cell Membrane / Q000201:enzymology / Q000378:metabolism; D006152:Cyclic GMP / Q000378:metabolism*; D066298:In Vitro Techniques; D007700:Kinetics; D008565:Membrane Proteins / Q000378:metabolism; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism; D010786:Photoreceptor Cells / Q000378:metabolism*; D011485:Protein Binding; D012374:Rod Cell Outer Segment / Q000201:enzymology / Q000378:metabolism*
D002147:Calmodulin; D008565:Membrane Proteins; D010727:Phosphoric Diester Hydrolases; D006152:Cyclic GMP; D002118:Calcium
cGMP-sviazyvaiushchie tsentry v fotoretseptornykh membranakh.