Detection of Ca2+ -dependent cyclic GMP binding protein in frog rod outer segments

FEBS Letters ◽  
1987 ◽  
Vol 219 (2) ◽  
pp. 293-295 ◽  
Author(s):  
Takao Shinozawa ◽  
Shoichi Terada ◽  
Hiroshi Matsusaka ◽  
Shinsuke Yamashita
Keyword(s):  
Cyclic Gmp ◽  
Binding Protein ◽  
Rod Outer Segments ◽  
Outer Segments

scholarly journals Light-activated hydrolysis of GTP and cyclic GMP in the rod outer segments.

1978 ◽  
Vol 279 (1) ◽  
pp. 55-69 ◽  
Author(s):  
E Bignetti ◽  
A Cavaggioni ◽  
R T Sorbi
Keyword(s):  
Cyclic Gmp ◽  
Rod Outer Segments ◽  
Outer Segments ◽  
Hydrolysis Of

Photoreceptor rod outer segment 48-kDa protein has ATPase activity

1990 ◽  
Vol 5 (6) ◽  
pp. 585-589 ◽  
Author(s):  
Ari Sitaramayya ◽  
Shereen Hakki
Keyword(s):  
Atpase Activity ◽  
Cyclic Gmp ◽  
Slow Rate ◽  
Binding Protein ◽  
Rod Outer Segments ◽  
Light Activation ◽  
Visual Transduction ◽  
Gtp Binding Protein ◽  
Gtp Binding

AbstractThe role of 48-kDa protein in Visual transduction remains unresolved. Two hypotheses for its role in quenching the light activation of cyclic GMP cascade suggest that the protein binds to either phosphodiesterase or phosphorylated rhodopsin. Since the protein is also reported to bind ATP, we anticipated that the protein may have ATP hydrolyzing activity, and in analogy with the GTP-binding protein of the rod outer segments, such activity may be greatly enhanced by the elements of transduction cyclic GMP cascade, permitting the protein to function cyclically as GTP-binding protein does. We found that purified 48-kDa protein hydrolyzes ATP but at a slow rate of 0.04–0.05 per min. The Km for ATP is about 45–65 μM. The activity is inhibited noncompetitively by ADP with a Ki of about 50 μM. The ATPase activity of 48-kDa protein is not affected by rhodopsin, bleached rhodopsin, phosphorylated rhodopsin, unactivated cyclic GMP phosphodiesterase, or phosphodiesterase (PDE) activated by GMP PNP-bound G-protein. These data show that although 48-kDa protein has ATPase activity, lack of regulation of this activity by the elements of visual transduction makes it unlikely for this activity to have a role in quenching the light activation of cyclic GMP cascade.

scholarly journals The GTP-binding protein of rod outer segments. I. Role of each subunit in the GTP hydrolytic cycle.

1987 ◽  
Vol 262 (19) ◽  
pp. 9316-9323 ◽  
Author(s):  
A Yamazaki ◽  
M Tatsumi ◽  
D C Torney ◽  
M W Bitensky
Keyword(s):  
Binding Protein ◽  
Rod Outer Segments ◽  
Gtp Binding Protein ◽  
Outer Segments ◽  
Gtp Binding

Cyclic GMP stimulation of a light-activated ATPase in rod outer segments

Nature ◽  
1983 ◽  
Vol 304 (5928) ◽  
pp. 733-735 ◽  
Author(s):  
T. J. Borys ◽  
R. Uhl ◽  
E. W. Abrahamson
Keyword(s):  
Cyclic Gmp ◽  
Rod Outer Segments ◽  
Outer Segments ◽  
Stimulation Of

scholarly journals Fast Ionic Flux Activated by Cyclic GMP in the Membrane of Cattle Rod Outer Segments

1983 ◽  
Vol 132 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Antonio CARETTA ◽  
Andrea CAVAGGIONI
Keyword(s):  
Cyclic Gmp ◽  
Rod Outer Segments ◽  
Ionic Flux ◽  
Outer Segments
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