Detection of cyclic GMP binding protein and ion channel activity in frog rod outer segments.

Szczegóły
Abstrakt

Tytuł:: Detection of cyclic GMP binding protein and ion channel activity in frog rod outer segments.
Autorzy:: Shinozawa T; Department of Natural Science, Naruto University of Teacher Education, Tokushima.
Sokabe M
Terada S
Matsusaka H
Yoshizawa T
Źródło:: Journal of biochemistry [J Biochem] 1987 Aug; Vol. 102 (2), pp. 281-90.
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
Język:: English
Imprint Name(s):: Publication: : Abingdon, UK : Oxford University Press
Original Publication: Tokyo : Japanese Biochemical Society
MeSH Terms:: Intracellular Signaling Peptides and Proteins*
Carrier Proteins/*metabolism
Cyclic GMP/*metabolism
Ion Channels/*metabolism
Photoreceptor Cells/*metabolism
Rod Cell Outer Segment/*metabolism
Animals ; Carrier Proteins/isolation & purification ; Cell Membrane/metabolism ; Ion Channels/physiology ; Light ; Lipid Bilayers ; Membrane Potentials ; Molecular Weight ; Phosphorylation ; Rana catesbeiana
Substance Nomenclature:: 0 (Carrier Proteins)
0 (Intracellular Signaling Peptides and Proteins)
0 (Ion Channels)
0 (Lipid Bilayers)
0 (cyclic GMP-binding protein)
H2D2X058MU (Cyclic GMP)
Entry Date(s):: Date Created: 19870801 Date Completed: 19871217 Latest Revision: 20190510
Update Code:: 20240104
DOI:: 10.1093/oxfordjournals.jbchem.a122052
PMID:: 2444580
: Czasopismo naukowe

In order to identify the cGMP-sensitive ion channel protein in frog rod outer segments (ROS), we analyzed cGMP binding proteins in the ROS by means of photoaffinity labeling with [3H]cGMP. We found four cGMP binding proteins with molecular weights (Mws) of 250K, 100K, 92K, and 53K. The 250K protein was an integral-membrane protein, which we named cG-Protein, (cG stands for cGMP). The cGMP-binding to cG-Protein was slightly increased by CaCl2. cG-Protein has a carbohydrate moiety. The amount of cG-Protein per single rod outer segment was estimated to be 9.0 x 10(6) molecules. Light-dependent phosphorylation of cG-Protein with [gamma-32P]ATP was observed. The 100K and 92K proteins were peripheral-membrane proteins, corresponding to cGMP phosphodiesterase. The 53K protein was a soluble protein. Incorporation of a membrane protein fraction of frog ROS into a planar lipid bilayer resulted in the appearance of at least three kinds of ion channel activities; two of them were related to cGMP. The possibility that cG-Protein is the cGMP-sensitive ion channel in vivo is discussed.

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