Linked Life Data

6238635

Source:http://linkedlifedata.com/resource/pubmed/id/6238635

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1985-1-4
pubmed:abstractText
The rate of thermal denaturation of bovine and rat opsin in the photoreceptor membranes was studied within a wide temperature range (between 37 and 70 degrees C). It was found that the rate of thermal denaturation of opsin at a physiological temperature (37 degrees C) might be commensurable or even exceed the known rate of rhodopsin renewal produced by photoreceptor disk formation and shedding. Lipid peroxidation caused an increase in the rate of opsin denaturation at a physiological temperature. It is assumed that accumulation of denatured opsin in the photoreceptor membranes during raised illumination together with lipid peroxidation induction may be one of the mechanisms leading to vision deterioration under raised illumination.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0365-9615
pubmed:author
pubmed:issnType
Print
pubmed:volume
98
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
396-8
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
[Heat denaturation of opsin in warm-blooded animals as a possible mechanism of light-induced retinal damage].
pubmed:publicationType
Journal Article, English Abstract