Nontransducing rhodopsin.
نویسندگان
چکیده
منابع مشابه
Nontransducing rhodopsin
Rhodopsin is converted by light to an active photoproduct that triggers the transduction cascade. The active photoproduct must then be inactivated by some kind of chemical modification. The question addressed here is whether photoconversion of the inactive photoproduct to rhodopsin creates a modified form of rhodopsin that is unable to support transduction. This question was investigated in ult...
متن کاملStudies in rhodopsin. VI. Regeneration of rhodopsin.
reducing power of steroids. The low pH of the reagent, which is responsible for hydrolysis of the cellulose, cannot be raised materially without seriously affecting the sensitivity. The latter depends on the formation of the yellow arsenomolybdate complex which requires a large excess of acid. In the experience of the author, variations of the blank value and serious disagreement between duplic...
متن کاملRhodopsin 7–The unusual Rhodopsin in Drosophila
Rhodopsins are the major photopigments in the fruit fly Drosophila melanogaster. Drosophila express six well-characterized Rhodopsins (Rh1-Rh6) with distinct absorption maxima and expression pattern. In 2000, when the Drosophila genome was published, a novel Rhodopsin gene was discovered: Rhodopsin 7 (Rh7). Rh7 is highly conserved among the Drosophila genus and is also found in other arthropods...
متن کاملBathorhodopsin intermediates from 11-cis-rhodopsin and 9-cis-rhodopsin.
Bathorhodopsin-rhodopsin difference spectra of native 11-cis-rhodopsin and regenerated 9-cis-rhodopsin were measured at room temperature with a double-beam laser spectrophotometer after excitation at 532 nm. A detailed analysis of data obtained at 85 psec after excitation suggests that the bathorhodopsins generated from 11-cis- and 9-cis-rhodopsin differ in their extinction coefficients and tha...
متن کاملLipid-rhodopsin hydrophobic mismatch alters rhodopsin helical content.
The ability of photoactivated rhodopsin to achieve the enzymatically active metarhodopsin II conformation is exquisitely sensitive to bilayer hydrophobic thickness. The sensitivity of rhodopsin to the lipid matrix has been explained by the hydrophobic matching theory, which predicts that lipid bilayers adjust elastically to the hydrophobic length of transmembrane helices. Here, we examined if b...
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: 1987
ISSN: 0022-1295,1540-7748
DOI: 10.1085/jgp.90.4.575