Cation selectivity of and cation binding to the cGMP-dependent channel in bovine rod outer segment membranes.
نویسندگان
چکیده
منابع مشابه
Cation selectivity of and cation binding to the cGMP-dependent channel in bovine rod outer segment membranes
The properties of the cGMP-dependent channel present in membrane vesicles prepared from intact isolated bovine rod outer segments (ROS) were investigated with the optical probe neutral red. The binding of neutral red is sensitive to transport of cations across vesicular membranes by the effect of the translocated cations on the surface potential at the intravesicular membrane/water interface (S...
متن کاملPhospholipid domains in bovine retinal rod outer segment disk membranes.
Phospholipid behavior in bovine retinal rod outer segment disk membranes and in phosphatidylcholine membranes containing the photopigment rhodopsin is explored. 31P NMR spectra of these systems show two distinguishable resonances. One resembles closely the 31P NMR resonance normally obtained from phospholipid bilayers. The other resonance is much broader. Thus, there appear to be two phospholip...
متن کاملExtrinsic Cation Selectivity of 2D Membranes
From a systematic study of the concentration driven diffusion of positive and negative ions across porous 2D membranes of graphene and hexagonal boron nitride (h-BN), we prove their cation selectivity. Using the current-voltage characteristics of graphene and h-BN monolayers separating reservoirs of different salt concentrations, we calculate the reversal potential as a measure of selectivity. ...
متن کاملSubmembrane assembly and renewal of rod photoreceptor cGMP-gated channel: insight into the actin-dependent process of outer segment morphogenesis.
The photoreceptor outer segment (OS) is comprised of two compartments: plasma membrane (PM) and disk membranes. It is unknown how the PM renewal is coordinated with that of the disk membranes. Here we visualized the localization and trafficking process of rod cyclic nucleotide-gated channel α-subunit (CNGA1), a PM component essential for phototransduction. The localization was visualized by fus...
متن کاملGARP2 accelerates retinal degeneration in rod cGMP-gated cation channel β-subunit knockout mice
The Cngb1 locus-encoded β-subunit of rod cGMP-gated cation channel and associated glutamic acid rich proteins (GARPs) are required for phototransduction, disk morphogenesis, and rod structural integrity. To probe individual protein structure/function of the GARPs, we have characterized several transgenic mouse lines selectively restoring GARPs on a Cngb1 knockout (X1-/-) mouse background. Optic...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of General Physiology
سال: 1990
ISSN: 0022-1295,1540-7748
DOI: 10.1085/jgp.96.3.517