Literature DB >> 3038605

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

T Shinozawa, S Terada, H Matsusaka, S Yamashita.   

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 phosphodiesterase.

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Year:  1987        PMID: 3038605     DOI: 10.1016/0014-5793(87)80238-7

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  2 in total

1.  Specific labeling and permanent activation of the retinal rod cGMP-activated channel by the photoaffinity analog 8-p-azidophenacylthio-cGMP.

Authors:  R L Brown; W V Gerber; J W Karpen
Journal:  Proc Natl Acad Sci U S A       Date:  1993-06-01       Impact factor: 11.205

2.  Detection and localization of a putative cyclic-GMP-activated channel protein in the protozoan ciliate Stentor coeruleus.

Authors:  M Walerczyk; H Fabczak; S Fabczak
Journal:  Protoplasma       Date:  2006-05-03       Impact factor: 3.186

  2 in total

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