Phosphatidate phosphatase activity in isolated rod outer segment from bovine retina

1986 ◽  
Vol 875 (2) ◽  
pp. 195-202 ◽  
Author(s):  
Susana J.Pasquaré de Garcia ◽  
Norma M. Giusto
Keyword(s):  
Phosphatase Activity ◽  
Outer Segment ◽  
Phosphatidate Phosphatase ◽  
Rod Outer Segment ◽  
Bovine Retina

scholarly journals First 3D-Structural Data of Full-length Guanylyl Cyclase 1 in Rod-Outer-Segment Preparations of Bovine Retina by Cross-linking/Mass Spectrometry

2021 ◽  
pp. 166947
Author(s):  
Anne Rehkamp ◽  
Dirk Tänzler ◽  
Christian Tüting ◽  
Panagiotis L. Kastritis ◽  
Claudio Iacobucci ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Guanylyl Cyclase ◽  
Outer Segment ◽  
Structural Data ◽  
Full Length ◽  
Cross Linking ◽  
Rod Outer Segment ◽  
Bovine Retina

Molar absorptivities of bovine retina rod outer segment phospholipids in n-hexane

1985 ◽  
Vol 151 (2) ◽  
pp. 409-417 ◽  
Author(s):  
C.N. N'Soukpoé-Kossi ◽  
C. Salesse ◽  
R.M. Leblanc ◽  
F. Boucher
Keyword(s):  
Outer Segment ◽  
Rod Outer Segment ◽  
Bovine Retina

scholarly journals First 3D-Structural Data of Full-length Rod-Outer-Segment Guanylyl Cyclase 1 in Bovine Retina by Cross-linking/Mass Spectrometry

2020 ◽  
Author(s):  
Anne Rehkamp ◽  
Dirk Tänzler ◽  
Christian Tüting ◽  
Panagiotis L. Kastritis ◽  
Claudio Iacobucci ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Structural Analysis ◽  
Guanylyl Cyclase ◽  
Outer Segment ◽  
Structural Data ◽  
Full Length ◽  
Cross Linking ◽  
Rod Outer Segment ◽  
Bovine Retina ◽  
Activity Measurements

AbstractThe rod-outer-segment guanylyl cyclase 1 (ROS-GC1) is a key transmembrane protein for retinal phototransduction. Mutations of ROS-GC1 correlate with different retinal diseases that often lead to blindness. No structural data are available for ROS-GC1 so far. We performed a 3D-structural analysis of native ROS-GC1 from bovine retina by cross-linking/mass spectrometry (XL-MS) and computational modeling. Absolute quantification and activity measurements of native ROS-GC1 were performed by MS-based assays directly in bovine retina samples. Our data present the first 3D-structural analysis of active, full-length ROS-GC1 in bovine retina. We propose a novel domain organization for the intracellular domain ROS-GC1. Our XL-MS data reveal that the α-helical domain connecting the kinase homology and catalytic domains can acquire different conformations. Also, the XL-MS data of native ROS-GC1 in bovine retina agree with a dimeric architecture. Our integrated approach can serve as a blueprint for conducting 3D-structural studies of membrane proteins in their native environment.

High time resolution enzyme cytochemistry of rod outer segment

1990 ◽  
Vol 48 (3) ◽  
pp. 878-879
Author(s):  
Takuma Saito ◽  
Toshihiro Takizawa
Keyword(s):  
Enzyme Activities ◽  
Outer Segment ◽  
Rapid Change ◽  
High Time Resolution ◽  
Visual Cell ◽  
Enzyme Cytochemistry ◽  
Activation Effect ◽  
Rod Outer Segment ◽  
Enzymatic Cascades ◽  
Rapid Drop

Cells and tissues live on a number of dynamic metabolic pathways, which are made up of sequential enzymatic cascades.Recent biochemical and physiological studies of vision research showed the importance of cGMP metabolism in the rod outer segment of visual cell, indicat ing that the photon activated rhodopsin exerts activation effect on the GTP binding protein, transducin, and this act ivated transducin further activates phosphodiesterase (PDEase) to result in a rapid drop in cGMP concentration in the cytoplasm of rod outer segment. This rapid drop of cGMP concentration exerts to close the ion channel on the plasma membrane and to stop of inward current brings hyperpolarization and evokes an action potential.These sequential change of enzyme activities, known as cGMP cascade, proceeds quite rapidly within msec order. Such a rapid change of enzyme activities, such as PDEase in rod outer segment, was not a matter of conventional histochemical invest igations.

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