Influence of GDP on interaction of transducin with cyclic nucleotide phosphodiesterase and rhodopsin from bovine retinal rods
In the presence of guanine nucleotides and rhodopsin-containing membranes from bovine retinal rod outer segments transducin stimulates light-sensitive cyclic nucleotide phosphodiesterase 5.5- to 7-fold. The activation constant (K/sub act/) for GTP and Gpp(NH)p is equal to 0.25 ..mu..M, while that for GDP and GDP..beta..S is 14 and 110 ..mu..M, respectively. GDP free of admixtures of other nucleotides does not activate phosphodiesterase at concentrations up to 1 mM, but is bound to transducin and inhibits the Gpp(NH)p-dependent activation of phosphodiesterase. The nature of the interaction of transducin with depolarized rhodopsin also depends on the type of guanine nucleotide bound: in the presence of GDP rhodopsin-containing membranes bind 70-100% of the transducin, whereas in the presence of Gpp(NH)p only 13% of the protein is bound. The data obtained indicate that GDP and GTP convert transducin to two different functional states: the transducin-GTP complex is bound to phosphodiesterase and activates it, while the transducin-GDP complex is bound primarily to rhodopsin.
- OSTI ID:
- 5629692
- Journal Information:
- Biochemistry (Engl. Transl.); (United States), Journal Name: Biochemistry (Engl. Transl.); (United States) Vol. 51:6; ISSN BIORA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
59 BASIC BIOLOGICAL SCIENCES
AMP
ANIMALS
BINDING ENERGY
BIOCHEMISTRY
BIOLOGICAL EFFECTS
BODY
BODY AREAS
CATTLE
CHEMISTRY
COMPLEXOMETRY
DOMESTIC ANIMALS
ENERGY
ENZYME ACTIVITY
ENZYME INHIBITORS
ENZYMES
ESTERASES
EYES
FACE
HEAD
HYDROLASES
ISOTOPE APPLICATIONS
LABELLED COMPOUNDS
LABELLING
LIGANDS
MAMMALS
METABOLIC ACTIVATION
NUCLEOTIDES
ORGANIC COMPOUNDS
ORGANS
PHOSPHODIESTERASES
PHOTOSENSITIVITY
PIGMENTS
PROTEINS
RETINA
RHODOPSIN
RUMINANTS
SENSE ORGANS
SENSITIVITY
STIMULATION
TRACER TECHNIQUES
TRITIUM COMPOUNDS
VERTEBRATES