title: [Guanosine triphosphate complex in rod outer segments of the frog retina].
abstract: It is shown that nearly 70% water--soluble protein of the frog retina outer segments (ROS) consist of three polypeptides with molecular weights 39 000, 36 000 and less than 15 000 daltons. These proteins are present in equal proportions and are, apparently, the subunits of a tightly bound protein complex. The subunit of 39 000 daltons is responsible for guanyl nucleotides binding. Parameters of the investigated GTP-binding complex are similar to transducyn which transmits excitation from bleached rhodopsin to PDE molecules in the bovine retina ROS. The thermodynamic state of GTP-binding protein in frog retina ROS depends on the functional state of the photoreceptor membrane, as shown by microcalorimetric method.
mesh_terms: D000262:Adenylyl Cyclases / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D019204:GTP-Binding Proteins; D008027:Light; D008970:Molecular Weight; D010786:Photoreceptor Cells / Q000378:metabolism*; D011896:Rana temporaria; D011956:Receptors, Cell Surface / Q000302:isolation & purification / Q000378:metabolism*; D012243:Rhodopsin / Q000378:metabolism; D012374:Rod Cell Outer Segment / Q000378:metabolism*; D013045:Species Specificity
chemical_list: D011956:Receptors, Cell Surface; D012243:Rhodopsin; D019204:GTP-Binding Proteins; D000262:Adenylyl Cyclases
vernacular_title: Guanizin-trifosfatnyĭ kompleks v naruzhnykh segmentakh palochek setchatki liagushki.