Detection of Ca2+-dependent cyclic GMP binding protein in frog rod outer segments
- 27 July 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 219 (2) , 293-295
- https://doi.org/10.1016/0014-5793(87)80238-7
Abstract
For the identification of the cGMP-sensitive ion channel protein of frog rod outer segments (ROS), we analyzed cGMP binding proteins in the ROS by photoaffinity labeling with [3H]cGMP. We found three cGMP binding polypeptides (66 kDa, 92 kDa and 100 kDa) in the membrane protein fraction of ROS. cGMP binding to the 66 kDa polypeptide required the addition of 2 mM CaCl2. We propose that this polypeptide corresponds to the cGMP-activated channel protein reported by Cook et al. [(1987) Proc. Natl. Acad. Sci. USA 84, 585–589]. The 100 kDa and 92 kDa polypeptides are subunits of the cGMP phosphodiesteraseKeywords
This publication has 5 references indexed in Scilit:
- Identification, purification, and functional reconstitution of the cyclic GMP-dependent channel from rod photoreceptors.Proceedings of the National Academy of Sciences, 1987
- Control of the light-regulated current in rod photoreceptors by cyclic GMP, calcium, and l-cis-diltiazem.Proceedings of the National Academy of Sciences, 1986
- Direct photoaffinity labeling of tubulin with guanosine 5'-triphosphateBiochemistry, 1985
- Induction by cyclic GMP of cationic conductance in plasma membrane of retinal rod outer segmentNature, 1985
- Electrical activity of vertebrate photoreceptorsQuarterly Reviews of Biophysics, 1970