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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
27
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pubmed:dateCreated |
1991-8-12
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pubmed:abstractText |
Absorption of a photon by the visual pigment rhodopsin leads to the formation of an activated conformational state, denoted rho*, which is capable of activating the visual G-protein, Gt. The bleaching of rhodopsin can be resolved into a series of spectrally distinct photointermediates. Previous studies suggest that the photointermediate metarhodopsin II (meta II, lambda max of 380 nm) corresponds to the physiologically active form rho*. In the studies reported herein, spectral and enzymological data were analyzed and compared so as to evaluate the temporal correspondence between meta II and rho*. This information was obtained by direct observation of the meta II and rho* decay times in parallel experiments utilizing identical preparations of urea-stripped, bovine retinal rod outer segment disk membranes at pH 8.0, 20 degrees C. Postflash spectra were deconvolved to resolve the meta II absorbance at 380 nm, and a decay time for the loss of meta II of 8.2 min (SD = 0.5 min) was obtained from fitting these data to a single-exponential decay process. The diminishing ability of bleached rhodopsin to activate Gt was measured by monitoring the level of catalyzed exchange of Gt-bound GDP for a nonhydrolyzable GTP analogue. Analysis of the decrease in the initial velocity of nucleotide exchange, measured at various postflash incubation times, yielded a rho* decay time of 7.7 min (SD = 0.5 min) when analyzed as a single-exponential process. The similarity of these decay times provides direct evidence that meta II and rho* are present over the same time regime, and further supports the equivalence of these two forms of photoactivated rhodopsin.(ABSTRACT TRUNCATED AT 250 WORDS)
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6761-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:1905955-Animals,
pubmed-meshheading:1905955-Cattle,
pubmed-meshheading:1905955-GTP-Binding Proteins,
pubmed-meshheading:1905955-Hydrolysis,
pubmed-meshheading:1905955-Photochemistry,
pubmed-meshheading:1905955-Protein Conformation,
pubmed-meshheading:1905955-Rhodopsin,
pubmed-meshheading:1905955-Spectrum Analysis
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pubmed:year |
1991
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pubmed:articleTitle |
Functional equivalence of metarhodopsin II and the Gt-activating form of photolyzed bovine rhodopsin.
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pubmed:affiliation |
Department of Biochemistry, University of Virginia Health Sciences Center, Charlottesville 22908.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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