Results 191 to 200 of about 15,771 (212)
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Pineal Opsin: a Nonvisual Opsin Expressed in Chick Pineal

Science, 1995
Pineal opsin (P-opsin), an opsin from chick that is highly expressed in pineal but is not detectable in retina, was cloned by the polymerase chain reaction. It is likely that the P-opsin lineage diverged from the retinal opsins early in opsin evolution. The amino acid sequence of P-opsin is 42 to 46 percent identical to that of the retinal opsins.
M, Max   +6 more
openaire   +2 more sources

Monkey Opsins

2018
This case will examine the evolution of trichromatic vision in old world monkeys.
White, Peter   +4 more
openaire   +2 more sources

Optogenetic Potentials of Diverse Animal Opsins: Parapinopsin, Peropsin, LWS Bistable Opsin

2021
Animal opsin-based pigments are light-activated G-protein-coupled receptors (GPCRs), which drive signal transduction cascades via G-proteins. Thousands of animal opsins have been identified, and molecular phylogenetic and biochemical analyses have revealed the unexpected diversity in selectivity of G-protein activation and photochemical property.
Mitsumasa, Koyanagi   +5 more
openaire   +2 more sources

Opsins and mammalian photoentrainment

Cell and Tissue Research, 2002
Research over the past decade has provided overwhelming evidence that photoreception in the vertebrate eye is not confined to the rod and cone photoreceptors. It appears that photoreceptor cells within the inner retina provide irradiance information to a wide variety of different photosensory tasks including photoentrainment, pupillary constriction and
Bellingham, James, Foster, Russell G.
openaire   +3 more sources

Opsin for immunological studies

Current Eye Research, 1985
Opsin for immunological studies can be prepared free from S-antigen by affinity chromatography on Con A-Sepharose. This preparation, however, contains 2-6% Con A originating from the affinity medium. Con A as impurity disturbs lymphocyte transformation tests carried out with opsin as test antigen. We describe a method for the removal of Con A by immuno-
R M, Broekhuyse, E D, Kuhlmann
openaire   +2 more sources

A radioimmunoassay specific for opsin

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983
A radioimmunoassay is developed for bovine opsin using a rabbit antiserum against bovine rod outer segment membranes. The assay is specific for opsin. Rhodopsin, bacteriorhodopsin and hemoglobin do not show cross-reaction. It can be carried out rapidly, has a sensitivity of 0.01 pmol bovine opsin and gives accurate results, even in the presence of a ...
J J, Schalken   +3 more
openaire   +2 more sources

Non-Gaussian fluctuations in opsins

2013 22nd International Conference on Noise and Fluctuations (ICNF), 2013
We investigate conductance fluctuations of two transmembrane proteins, bacteriorhodopsin and proteorhodopsin, belonging to the family of opsins. These proteins are sensitive to visible light and are promising biomaterials for the realization of novel photodevices.
ALFINITO, ELEONORA   +2 more
openaire   +1 more source

Linkage of Retinal to Opsin

Nature New Biology, 1971
RHODOPSIN, the visual pigment of vertebrate rods, has been shown to consist of a chromophore (11-cis retinal) bound to a protein (opsin)1–2. It has been proposed that the linkage is a Schiff base between phosphatidyl ethanolaniine (PE) and retinal and that when exposed to light, the retinal migrates from PE to the e-amino-group of a lysine residue in ...
R T, Hoffman, M O, Hall, R E, Anderson
openaire   +2 more sources

Immunoreactivity of rhodopsin and opsin

Biochimica et Biophysica Acta (BBA) - General Subjects, 1984
An examination by a radioimmunoassay of the relative affinity of opsin and rhodopsin for rabbit antibody raised against bovine rhodopsin revealed that opsin was the preferred antigen. About 10-fold greater amounts of rhodopsin than opsin were required to achieve 50% inhibition of binding of 125I-labeled ligand in the RIA.
J J, Plantner, E L, Kean
openaire   +2 more sources

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